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<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="other" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Russian Journal of Infection and Immunity</journal-id><journal-title-group><journal-title xml:lang="en">Russian Journal of Infection and Immunity</journal-title><trans-title-group xml:lang="ru"><trans-title>Инфекция и иммунитет</trans-title></trans-title-group></journal-title-group><issn publication-format="print">2220-7619</issn><issn publication-format="electronic">2313-7398</issn><publisher><publisher-name xml:lang="en">SPb RAACI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">269</article-id><article-id pub-id-type="doi">10.15789/2220-7619-2015-1-15-26</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>REVIEWS</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>ОБЗОРЫ</subject></subj-group><subj-group subj-group-type="article-type"><subject></subject></subj-group></article-categories><title-group><article-title xml:lang="en">STRATEGY OF PROGRAMMED CELL DEATH IN PROKARYOTES</article-title><trans-title-group xml:lang="ru"><trans-title>СТРАТЕГИИ ПРОГРАММИРОВАННОЙ КЛЕТОЧНОЙ ГИБЕЛИ У ПРОКАРИОТ</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Andrukov</surname><given-names>B. G.</given-names></name><name xml:lang="ru"><surname>Андрюков</surname><given-names>Б. Г.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p/><p/><p/><p>PhD, MD (Medicine), Leading Researcher, Laboratory of Molecular Epidemiology and Microbiology, Somov Research Institute of Epidemiology and Microbiology, Siberian Branch of RAMS, Vladivostok, Russian Federation;</p></bio><bio xml:lang="ru"><p/><p/><p/><p>д.м.н., ведущий научный сотрудник лаборатории молекулярной эпидемиологии и микробиологии ФГБУ НИИЭМ им. Г.П. Сомова СО РАМН, г. Владивосток, Россия;</p></bio><email>andrukov_bg@mail.ru</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Somova</surname><given-names>L. M.</given-names></name><name xml:lang="ru"><surname>Сомова</surname><given-names>Л. М.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p/><p/><p/><p>PhD, MD (Medicine), Professor, Director of Somov Research Institute of Epidemiology and Microbiology, Siberian Branch of RAMS, Vladivostok, Russian Federation;</p></bio><bio xml:lang="ru"><p/><p/><p/><p>д.м.н., профессор, директор ФГБУ НИИЭМ им. Г.П. Сомова СО РАМН, г. Владивосток, Россия; </p></bio><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Timchenko</surname><given-names>N. F.</given-names></name><name xml:lang="ru"><surname>Тимченко</surname><given-names>Н. Ф.</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p/><p/><p/><p>PhD, MD (Medicine), Professor, Leading Researcher, Laboratory of Molecular Epidemiology and Microbiology, Somov Research Institute of Epidemiology and Microbiology, Siberian Branch of RAMS, Vladivostok, Russian Federation.</p></bio><bio xml:lang="ru"><p/><p/><p/><p>д.м.н., профессор, ведущий научный сотрудник лаборатории молекулярной эпидемиологии и микробиологии ФГБУ НИИЭМ им. Г.П. Сомова СО РАМН, г. Владивосток, Россия. </p></bio><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">690087, Russian Federation, Vladivostok, Selskaya str., 1, Somov Research Institute of Epidemiology and Microbiology, Siberian Branch of RAMS.</institution></aff><aff><institution xml:lang="ru">690087, Россия, г. Владивосток, ул. Сельская, 1, ФГБУ НИИЭМ им. Г.П. Сомова СО РАМН.</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2015-04-21" publication-format="electronic"><day>21</day><month>04</month><year>2015</year></pub-date><volume>5</volume><issue>1</issue><issue-title xml:lang="en"/><issue-title xml:lang="ru"/><fpage>15</fpage><lpage>26</lpage><history><date date-type="received" iso-8601-date="2015-04-21"><day>21</day><month>04</month><year>2015</year></date><date date-type="accepted" iso-8601-date="2015-04-21"><day>21</day><month>04</month><year>2015</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2015, Andrukov B.G., Somova L.M., Timchenko N.F.</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2015, Андрюков Б.Г., Сомова Л.М., Тимченко Н.Ф.</copyright-statement><copyright-year>2015</copyright-year><copyright-holder xml:lang="en">Andrukov B.G., Somova L.M., Timchenko N.F.</copyright-holder><copyright-holder xml:lang="ru">Андрюков Б.Г., Сомова Л.М., Тимченко Н.Ф.</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/><license><ali:license_ref xmlns:ali="http://www.niso.org/schemas/ali/1.0/">https://creativecommons.org/licenses/by/4.0</ali:license_ref></license></permissions><self-uri xlink:href="https://iimmun.ru/iimm/article/view/269">https://iimmun.ru/iimm/article/view/269</self-uri><abstract xml:lang="en"><p>Programmed cell death (PCD) was first studied in eukaryotic organisms. This system also operates in the development life cycle of prokaryotes. The system PCD in microorganisms is activated a wide range of signals in response to the stresses associated with adverse environmental conditions or exposure to antibacterial agents. The results of numerous studies in the past decade allow considering the system PCD in prokaryotes as an evolutionary conservation of the species. These results significantly expanded understanding of the role of PCD in microorganisms and opened a number of important areas of research of the morphological and molecular genetic approaches to the study of death strategies for the survival in bacterial populations. The purpose of the review is to summarize the morphological and molecular genetic characteristics of PCD in prokaryotes which are real manifestations of the mechanisms of this phenomenon. </p></abstract><trans-abstract xml:lang="ru"><p>Программированная гибель клеток (ПГК) была впервые изучена в эукариотических организмах. Эта система также функционирует в процессе развития прокариот. Система ПГК у микроорганизмов активируется широким спектром сигналов в ответ на стрессы, связанные с неблагоприятными условиями окружающей среды или воздействием антибактериальных средств. Результаты многочисленных исследований, проведенных в последнее десятилетие, позволяют рассматривать систему ПГК у прокариот как средство эволюционного сохранения вида. Эти результаты существенно расширили представления о роли ПГК у микроорганизмов и открыли ряд важных направлений исследований, морфологических и молекулярно-генетических подходов к изучению стратегий смерти ради выживания у бактериальных популяций. Цель обзора: обобщение сведений о морфологических и молекулярно-генетических признаках ПГК у прокариот, являющихся реальными проявлениями механизмов этого феномена. </p></trans-abstract><kwd-group xml:lang="en"><kwd>prokaryotes</kwd><kwd>apoptosis</kwd><kwd>autolysis</kwd><kwd>necrosis</kwd><kwd>piroptosis</kwd><kwd>markers</kwd><kwd>antibiotics</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>прокариоты</kwd><kwd>апоптоз</kwd><kwd>аутолиз</kwd><kwd>некроз</kwd><kwd>пироптоз</kwd><kwd>маркеры</kwd><kwd>антибиотики</kwd></kwd-group><funding-group/></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>1. Абатуров А.Е., Волосовец А.П., Юлиш Е.И. Роль NOD-подобных рецепторов в рекогниции патоген-ассоциированных молекулярных структур инфекционных патогенных агентов и развитии воспаления. Здоровье ребенка (Украина). 2013. Т. 47, No 4. С. 7–13. [Abaturov A.E., Volosovets A.P., Yulish E.I. The role of NOD-like receptor in recognition of pathogenassociated molecular structures of infectious pathogens and the development of inflammation. Zdorov’e rebenka (Ukraina) = Child Health (Ukraine), 2013, vol. 47, no. 4, pp. 7–13. (In Russ.)]</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>2. Андрюков Б.Г., Тимченко Н.Ф. Апоптоз-модулирующие стратегии детерминант патогенности иерсиний // Здоровье. Медицинская экология. Наука. 2015. Т. 59, No 1. С. 29–40. [Andryukov B.G., Timchenko N.F. Apoptosis-modulating strategy determinants of virulence of Yersinia. Zdorov’e. Meditsinskaya ekologiya. Nauka = Health. Medical ecology. Science, 2015, vol. 59, no. 1, pp. 29–40. (In Russ.)]</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>3. Сомова Л.М., Бузолева Л.С., Исаченко А.С., Сомов Г.П. Адаптивные ультраструктурные изменения бактерий Yersinia pseudotuberculosis при обитании в почве // Журнал микробиологии, эпидемиологии и иммунобиологии. 2006. No 3. С. 36–40. [Somova L.M., Buzoleva L.S., Isachenko A.S., Somov G.P. Adaptive ultrastructural changes Yersinia pseudotuberculosis at habitation in soil. Zhurnal mikrobiologii, epidemiologii i immunobiologii = Journal of Microbiology, Epidemiology and Immunobiology, 2006, no. 3, pp. 36–40. (In Russ.)]</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>4. Сомова Л.М., Бузолева Л.С., Плехова Н.Г. Ультраструктура патогенных бактерий в разных экологических условиях. Владивосток: Медицина ДВ, 2009. 200 с. [Somova L.M., Buzoleva L.S., Plekhova N.G. Ul’trastruktura patogennykh bakterii v raznykh ekologicheskikh usloviyakh [Ultrastructure of pathogenic bacteria in different ecological conditions]. Vladivostok: Far East Medicine, 2009, 200 p.]</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>5. Ackermann S., Hiller S., Osswald H., Lösle M., Grenz A., Hambrock A. 17beta-estradiol modulates apoptosis in pancreatic betacells by specific involvement of the sulfonylurea receptor (SUR) isoform SUR1. J. Biol. Chem., 2009, vol. 284, no. 8, pp. 4905–4913.</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>6. Adler E., Barak I., Stragier P. Bacillus subtilis locus encoding a killer protein and its antidote. J. Bacteriol., 2001, vol. 183, pp. 3574–3581.</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>7. Aguiló N., Marinova D., Martín C., Pardo J. ESX-1-induced apoptosis during mycobacterial infection: to be or not to be, that is the question. Front Cell Infect. Microbiol., 2013, vol. 3, pp. 80–88.</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>8. Bos J., Yakhnina A.A., Gitai Z. BapE DNA endonuclease induces an apoptotic-like response to DNA damage in Caulobacter. Proc. Natl. Acad. Sci. USA, 2012, vol. 109, pp. 18096–18101.</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>9. Buts L., Lah J., Dao-Thi M.-H., Wyns L., Loris R. Toxin-antitoxin modules as bacterial metabolic stress managers. Trends Biochem. Sci., 2005, vol. 30, no. 12, pp. 672–679.</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>10. Camacho D.M., Kohanski M.A., Callura J.M., Collins J.J. Antibiotic-induced bacterial cell death exhibits physiological and biochemical hallmarks of apoptosis. Mol. Cell, 2012, vol. 46, no. 5, pp. 561–572.</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>11. Camougrand N., Kissová I., Velours G., Manon S. Uth1p: a yeast mitochondrial protein at the crossroads of stress, degradation and cell death. FEMS Yeast Res., 2004, vol. 5, no. 2, pp. 133–140.</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>12. Carmona-Gutierrez D., Eisenberg T., Buttner S., Meisinger C., Kroemer G., Madeo F. Apoptosis in yeast: triggers, pathways, subroutines. Cell Death Differ., 2010, vol. 17, no. 5, pp. 763–773.</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>13. Cellini L., Robuffo I., Maraldi N.M., Donelli G. Searching the point of no return in Helicobacter pylori life: necrosis and/or programmed death? J. Appl. Microbiol., 2001, vol. 90, pp. 727–732.</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>14. Chatterjee I., Neumayer D., Herrmann M. Senescence of staphylococci: using functional genomics to unravel the roles of ClpC ATPase during late stationary phase. Int. J. Med. Microbiol., 2010, vol. 300, no. 2–3, pp. 130–136.</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>15. Chaumorcel M., Lussignol M., Mouna L., Cavignac Y., Fahie K., Cotte-Laffitte J., Geballe A., Brune W., Beau I., Codogno P., Esclatine A. The human cytomegalovirus protein TRS1 inhibits autophagy via its interaction with Beclin 1. J. Virol., 2012, vol. 86, no. 5, pp. 2571–2584.</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>16. Christensen M.E., Jansen E.S., Sanchez W., Waterhouse N.J. Flow cytometry based assays for the measurement of apoptosisassociated mitochondrial membrane depolarisation and cytochrome c release. Methods, 2013, vol. 61, no. 2, pp. 138–145.</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>17. Christensen S.K., Pedersen K., Hansen F.G., Gerdes K. Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J. Mol. Biol., 2003, vol. 332, pp. 809–819.</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>18. D’Amelio M., Sheng M., Cecconi F. Caspase-3 in the central nervous system: beyond apoptosis. Trends Neurosci., 2012, vol. 35, no. 11, pp. 700–709.</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>19. Danelishvili L., Bermudez L.E. Analysis of pyroptosis in bacterial infection. Methods Mol. Biol., 2013, vol. 1004, pp. 67–73.</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>20. Danial N.N., Korsmeyer S.J. Cell death: critical control points. Cell, 2004, vol. 116, no. 2, pp. 205–219.</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>21. Declercq W., Vanden-Berghe T., Vandenabeele P. RIP kinases at the crossroads of cell death and survival. Cell, 2009, vol. 138, no. 2, pp. 229–232.</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>22. De la Cruz M. A., Zhao W., Farenc C., Gimenez G., Raoult D., Cambillau C., Gorvel J.-P., Méresse S. A toxin-antitoxin module of Salmonella promotes virulence in mice. PLOS pathogens, 2013, vol. 9, no. 12, p. e1003827.</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>23. Deleo V. Modulation of phagocyte apoptosis by bacterial pathogens. Apoptosis (London), 2004, vol. 9, pp. 399–413.</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>24. Denton D., Aung-Htut M.T., Kumar S., Baehrecke E.H. Developmentally programmed cell death in Drosophila. Biochim. Biophys. Acta, 2013, vol. 1833, no. 12, pp. 3499–3506.</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>25. Denton D., Chang T.K., Nicolson S., Shravage B., Simin R., Baehrecke E.H., Kumar S. Relationship between growth arrest and autophagy in midgut programmed cell death in Drosophila. Cell Death Differ., 2012, vol. 19, no. 8, pp. 1299–1307.</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>26. Dunin-Horkawicz S., Kopec K.O., Lupas A.N. Prokaryotic ancestry of eukaryotic protein networks mediating innate immunity and apoptosis. J. Mol. Biol., 2014, vol. 426, no. 7, pp.1568–1582.</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>27. Dwyer D.J., Kohanski M.A., Hayete B., Collins J.J. Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli. Mol. Syst. Biol., 2007, vol. 3, p. 91.</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>28. Eckardt J., Lorek M., Zimmer G. The fusion protein of respiratory syncytial virus triggers p53-dependent apoptosis. J. Virol., 2008, vol. 82, no. 7, pp. 3236–3249.</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>29. Engelberg-Kulka H., Amitai S., Reches M., Sat B., Hazan R. Bacterial programmed cell death as a target for antibiotics. Trends Microbiol., 2004, vol. 12, рр. 66–71.</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>30. Engelberg-Kulka H., Kolodkin-Gal I., Amitai S., Hazan R. Bacterial programmed cell death and multicellular behavior in bacteria. PLOS Genet., 2006, vol. 2, no. 10, p. e135.</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>31. Erental A., Idith Sh.I., Engelberg-Kulka H. Two programmed cell death systems in Escherichia coli: an apoptotic-like dеath is inhibited by the mazEF-mediated death pathway. PLOS Biology, 2012, vol. 10, no. 3, p. e1001281.</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>32. Fineran P.C., Blower T.R., Foulds I.J., Humphreys D.P., Lilley K.S. The phage abortive infection system, ToxIN, functions as a protein-RNA toxin-antitoxin pair. Proc. Natl. Acad. Sci. USA, 2009, vol. 106, pp. 894–899.</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>33. Fink S.L., Cookson B.T. Caspase-1-dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell Microbiol., 2006, vol. 8, no. 11, pp. 1812–1825.</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>34. Fu Z., Tamber S., Memmi G., Donegan N.P. Cheung A.L. Overexpression of MazFsa in Staphylococcus aureus induces bacteriostasis by selectively targeting mRNAs for cleavage. J. Bacteriol. 2012, vol. 191, pp. 2051–2059.</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>35. Galluzzi L., Kepp O., Krautwald S., Kroemer G., Linkermann A. Molecular mechanisms of regulated necrosis. Semin. Cell Dev. Biol., 2014, vol. 35, pp. 24–32.</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>36. Gautam S., Sharma A. Rapid cell death in Xanthomonas campestris pv. glycines. J. Gen. Appl. Microbiol., 2002, vol. 48, no. 2, pp. 67–76.</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>37. Gertz S., Engelmann S., Schmid R., Ohlsen K., Hacker J., Hecker M. Regulation of σB-dependent transcription of sigB and asp23 in two different Staphylococcus aureus strains. Mol. Gen. Genet., 1999, vol. 261, pp. 558–566.</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>38. Giansanti V., Torriglia A., Scovassi A.I. Conversation between apoptosis and autophagy: «Is it your turn or mine?». Apoptosis, 2011, vol. 16, no. 4, pp. 321–333.</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>39. Godoy V.G., Jarosz D.F., Walker F.L., Simmons L.A., Walker G. Y-family DNA polymerases respond to DNA damage-independent inhibition of replication fork progression. EMBO J., 2006, vol. 25, pp. 868–879.</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>40. Gómez-Fernández J.C. Functions of the C-terminal domains of apoptosis-related proteins of the Bcl-2 family. Chem. Phys. Lipids, 2014, vol. 183, pp. 77–90.</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>41. Goulard C., Langrand S., Chauvaux S. Yersinia pestis chromosome encodes active addiction toxins. J. Bacteriol., 2010, vol. 192, no. 14, pp. 3669–3677.</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>42. Green D.R., Oberst A., Dillon C.P., Weinlich R., Salvesen G.S. RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts. Mol. Cell, 2011, vol. 44, no. 1, pp. 9–16.</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>43. Guilhelmelli F., Vilela N., Albuquerque P., Derengowski L.D., Silva-Pereira I., Kyaw C.M. Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front Microbiol., 2013, vol. 4, 353 p.</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>44. Guiral S., Mitchell T.J., Martin B., Claverys J.P. Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements. Proc. Natl. Acad. Sci. USA, 2005, vol. 14, pp. 8710–8715.</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>45. Han K.D., Ahn D.H., Lee S.A., Min Y.H., Kwon A.R., Ahn H.C., Lee B.J. Identification of chromosomal HP0892-HP0893 toxin-antitoxin proteins in Helicobacter pylori and structural elucidation of their protein-protein interaction. J. Biol. Chem., 2013, vol. 288, no. 8, pp. 6004–6013.</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>46. Hayes F. Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest. Science, 2003, vol. 301, pp. 1496–1499.</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>47. Hayes F., Van Melderen L. Toxins-antitoxins: diversity, evolution and function. Crit. Rev. Biochem. Mol. Biol., 2011, vol. 46, no. 5, pp. 386–408.</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>48. Hazan R., Sat B., Engelberg-Kulka H. Escherichia coli mazEF-mediated cell death is triggered by various stressful conditions. J. Bacteriol., 2004, vol. 186, pp. 3663–3669.</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>49. Hotchkiss R.S., Strasser A., McDunn J.E., Swanson P.E. Cell death in disease: mechanisms and emerging therapeutic concepts. N. Engl. J. Med., 2009, vol. 361, pp. 1570–1583.</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>50. Kamat P.K., Kalani A., Kyles P., Tyagi S.C., Tyagi N. Autophagy of Mitochondria: A promising therapeutic target for neurodegenerative disease. Cell Biochem. Biophys., 2014, vol. 70, no. 2, pp. 707–719.</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>51. Kang J., Pervaiz S. Crosstalk between Bcl-2 family and Ras family small GTPases: potential cell fate regulation? Front Oncol., 2013, vol. 2, 206 p.</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>52. Kerr J.F., Wyllie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Brit. J. Cancer, 1972, vol. 26, pp. 239–257.</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>53. Klionsky D.J., Codogno P. The mechanism and physiological function of macroautophagy. J. Innate Immun., 2013, vol. 5, no. 5, pp. 427–433.</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>54. Kolodkin-Gal I., Sat B., Keshet A., Engelberg-Kulka H. The communication factor EDF and the toxin-antitoxin module mazEF determine the mode of action of antibiotics. PLOS Biol., 2008, vol. 16, no. 6, p. e319.</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>55. Koonin E.V., Aravind L. Origin and evolution of eukaryotic apoptosis: the bacterial connection. Cell Death Differ., 2002, vol. 9, no. 4, pp. 394–404.</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>56. Labbé K., Saleh M. Cell death in the host response to infection. Cell Death Differ., 2008, vol. 15, no. 9, pp. 1339–1349.</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>57. Leplae R., Geeraerts D., Hallez R., Guglielmini J., Drèze P. Diversity of bacterial type II toxin-antitoxin systems: a comprehensive search and functional analysis of novel families. Nucleic Acids Research, 2011, vol. 39, pp. 5513–5525.</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>58. Lewis K. Programmed death in bacteria. Microbiol. Mol. Biol. Rev., 2002, vol. 64, pp. 503–514.</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>59. Loewith R., Hall M.N. Target of rapamycin (TOR) in nutrient signaling and growth control. Genetics, 2011, vol. 189, no. 4, pp. 1177–1201.</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>60. Ludovico P. Overeating yeast display fatty acid-induced necrotic cell death. Cell Cycle, 2010, vol. 9, no. 15, 2929 p.</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>61. Makarova K.S., Wolf Y.I., Koonin E.V. Comprehensive comparative-genomic analysis of type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes. Biol. Direct., 2009, vol. 4, pp. 11–19.</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>62. Manteca A., Fernandez M., Sanchez J. Cytological and biochemical evidence for an early cell dismantling event in surface cultures of Streptomyces antibioticus. Res. Microbiol., 2006, vol. 157, no. 2, pp. 143–152.</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>63. Marino G., Niso-Santano M., Baehrecke E.H., Kroemer G. Self-consumption: the interplay of autophagy and apoptosis. Nature Rev. Mol. Cell Biol., 2014, vol. 15, pp. 81–94.</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>64. Marino M.L., Pellegrini P., Di Lernia G., Djavaheri-Mergny M., Brnjic S., Zhang X., Hägg M., Linder S., Fais S., Codogno P., De Milito A. Autophagy is a protective mechanism for human melanoma cells under acidic stress. J. Biol. Chem., 2012, vol. 287, no. 36, pp. 30664–30676.</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>65. Masuda H., Tan Q., Awano N., Wu K.P., Inouye M. YeeU enhances the bundling of cytoskeletal polymers of MreB and FtsZ, antagonizing the CbtA (YeeV) toxicity in Escherichia coli. Mol. Microbiol., 2012, vol. 84, pp. 979–989.</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>66. Mavrianos J., Berkow E.L., Desai C., Pandey A., Batish M., Rabadi M.J., Barker K.S., Pain D., Rogers P.D., Eugenin E.A., Chauhan N. Mitochondrial two-component signaling systems in Candida albicans. Eukaryot. Cell, 2013, vol. 12, no. 6, pp. 913–922.</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>67. Nancy A. Eukaryote programmed cell death in plants: a role for mitochondrial-associated hexokinases. Plant Cell, 2006, vol. 18, pp. 2097–2099.</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>68. Nariya H., Inouye M. MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development. Cell, 2008, vol. 32, pp. 55–66.</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>69. Nolle N., Schuster C.F., Bertram R. Two paralogous yefM-yoeB loci from Staphylococcus equorum encode functional toxinantitoxin systems. Microbiology, 2013, vol. 159, no. 8, pp. 1575–1585.</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>70. Norton J.P., Mulvey M.A. Toxin-antitoxin systems are important for niche-specific colonization and stress resistance of uropathogenic Escherichia coli. PLOS Pathog., 2012, vol. 8, p. e1002954.</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>71. Nyström T. Nonculturable bacteria: programmed survival forms or cells at death’s door? Bioessays, 2003, vol. 25, pp. 204–211.</mixed-citation></ref><ref id="B72"><label>72.</label><mixed-citation>72. Pandey D.P., Gerdes K. Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Research, 2005, vol. 33, pp. 966–976.</mixed-citation></ref><ref id="B73"><label>73.</label><mixed-citation>73. Park J.H., Yamaguchi Y., Inouye M. Bacillus subtilis MazF-bs (EndoA) is a UACAU-specific mRNA interferase. FEBS Lett., 2011, vol. 585, pp. 2526–2532.</mixed-citation></ref><ref id="B74"><label>74.</label><mixed-citation>74. Pedersen K., Christensen S.K., Gerdes K. Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol. Microbiol., 2002, vol. 45, pp. 501–510.</mixed-citation></ref><ref id="B75"><label>75.</label><mixed-citation>75. Port U., Brovkin V., Claussen M. The influence of vegetation dynamics on anthropogenic climate change. Earth Syst. Dynam., 2012, vol. 3, pp. 233–243.</mixed-citation></ref><ref id="B76"><label>76.</label><mixed-citation>76. Ramage H.R., Connolly L.E., Cox J.S. Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. PLOS Genet., 2009, vol. 5, p. e1000767.</mixed-citation></ref><ref id="B77"><label>77.</label><mixed-citation>77. Ramisetty B.C., Natarajan B., Santhosh R.S. MazEF-mediated programmed cell death in bacteria: «What is this?». Crit. Rev. Microbiol., 2015, vol. 41, no. 1, pp. 89–100.</mixed-citation></ref><ref id="B78"><label>78.</label><mixed-citation>78. Rice K.C., Bayles K.W. Molecular control of bacterial death and lysis. Microbiol. Mol. Biol. Rev., 2008, vol. 72, pp. 85–109.</mixed-citation></ref><ref id="B79"><label>79.</label><mixed-citation>79. Robertson C.L., Scafidi S., McKenna M.C., Fiskum G. Mitochondrial mechanisms of cell death and neuroprotection in pediatric ischemic and traumatic brain injury. Exp. Neurol., 2009, vol. 218, no. 2, pp. 371–380.</mixed-citation></ref><ref id="B80"><label>80.</label><mixed-citation>80. Rostovtseva T.K., Tan W., Colombini M. On the role of VDAC in apoptosis: fact and fiction. J. Bioenerg. Biomembr., 2005, vol. 37, pp. 129–142.</mixed-citation></ref><ref id="B81"><label>81.</label><mixed-citation>81. Rothenbacher F.P. Clostridium difficile MazF toxin exhibits selective, not global, mRNA cleavage. J. Bacteriol., 2012, vol. 194, pp. 3464–3474.</mixed-citation></ref><ref id="B82"><label>82.</label><mixed-citation>82. Ryter S.W., Mizumura K., Choi A.M. The impact of autophagy on cell death modalities. Int. J. Cell. Biol., 2014, vol. 2014, p. е502676.</mixed-citation></ref><ref id="B83"><label>83.</label><mixed-citation>83. Samejima K., Earnshaw W.C. Trashing the genome: the role of nucleases during apoptosis. Nat. Rev. Mol. Cell. Biol., 2005, vol. 6, no. 9, pp. 677–688.</mixed-citation></ref><ref id="B84"><label>84.</label><mixed-citation>84. Shamas-Din A., Brahmbhatt H., Leber B., Andrews D.W. BH3-only proteins: orchestrators of apoptosis. Biochim. Biophys. Acta, 2011, vol. 1813, no. 4, pp. 508–520.</mixed-citation></ref><ref id="B85"><label>85.</label><mixed-citation>85. Shemarova I.V. Phosphoinositide signaling in unicellular eukarуotes. Crit. Rev. Microbiol., 2007, vol. 33, pp. 141–156.</mixed-citation></ref><ref id="B86"><label>86.</label><mixed-citation>86. Søgaard-Andersen L., Yang Z. Programmed cell death: role for MazF and MrpC in Myxococcus multicellular development. Curr. Biol., 2008, vol. 18, pp. 337–339.</mixed-citation></ref><ref id="B87"><label>87.</label><mixed-citation>87. Tait S.W., Green D.R. Mitochondrial regulation of cell death. Cold Spring Harb. Perspect. Biol., 2013, vol. 5, no. 9, p. a008706.</mixed-citation></ref><ref id="B88"><label>88.</label><mixed-citation>88. Tanouchi Y., Lee A.J., Meredith H., You L. Programmed cell death in bacteria and implications for antibiotic therapy. Trends Microbiol., 2013, vol. 21, no. 6, рр. 265–270.</mixed-citation></ref><ref id="B89"><label>89.</label><mixed-citation>89. Ulukaya E., Acilan C., Yilmaz Y. Apoptosis: why and how does it occur in biology? Cell. Biochem. Funct., 2011, vol. 29, no. 6, pp. 468–480.</mixed-citation></ref><ref id="B90"><label>90.</label><mixed-citation>90. Van Loo G., Saelens X., Van Gurp M., MacFarlane M., Martin S.J., Vandenabeele P. The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet. Cell Death Differ., 2002, vol. 9, pp. 1031–1042.</mixed-citation></ref><ref id="B91"><label>91.</label><mixed-citation>91. Wang X., Lord D.M., Cheng H.Y., Osbourne D.O., Hong S.H. A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS. Nat. Chem. Biol., 2012, vol. 8, pp. 855–861.</mixed-citation></ref><ref id="B92"><label>92.</label><mixed-citation>92. Wardhawan S., Gautam S., Sharma A. Involvement of proline oxidase (PutA) in programmed cell death of Xanthomonas. PLOS One, 2014, vol. 9, no. 5, p. e96423.</mixed-citation></ref><ref id="B93"><label>93.</label><mixed-citation>93. Weely H., Yoshida R., Kudoh S., Hasegawa K., Niimori-Kita K., Ito T. Regulator of calcineurin 1-1L protects cardiomyocytes against hypoxia-induced apoptosis via mitophagy. Trends Microbiol., 2010, vol. 13, pp. 169–182.</mixed-citation></ref><ref id="B94"><label>94.</label><mixed-citation>94. Williams K., Gokulan K., Shelman D., Akiyama T., Khan A., Khare S. Cytotoxic mechanism of cytolethal distending toxin in nontyphoidal salmonella serovar (Salmonella javiana) during macrophage infection. DNA Cell Biol., 2015, vol. 34, no. 2, рр. 113–124.</mixed-citation></ref><ref id="B95"><label>95.</label><mixed-citation>95. Wu W., Liu P., Li J. Necroptosis: an emerging form of programmed cell death. Crit. Rev. Oncol. Hematol., 2012, vol. 82, no. 3, pp. 249–258.</mixed-citation></ref><ref id="B96"><label>96.</label><mixed-citation>96. Wu Y.C., Wang X., Xue D. Methods for studying programmed cell death in C. elegans. Methods Cell. Biol., 2012, vol. 10, pp. 295–320.</mixed-citation></ref><ref id="B97"><label>97.</label><mixed-citation>97. Yagüe P., López-García M.T., Rioseras B., Sánchez J.A. Pre-sporulation stages of Streptomyces differentiation: state-of-the-art and future perspectives. FEMS Microbiol. Lett., 2013, vol. 342, no. 2, pp. 79–88.</mixed-citation></ref><ref id="B98"><label>98.</label><mixed-citation>98. Yamaguchi Y., Park J.H., Inouye M. Toxin-antitoxin systems in bacteria and archaea. Annu. Rev. Genet., 2011, vol. 45, pp. 61–79.</mixed-citation></ref><ref id="B99"><label>99.</label><mixed-citation>99. Yuan J., Kroemer G. Alternative cell death mechanisms in development and beyond. Genes Dev., 2010, vol. 24, pp. 2592–2602.</mixed-citation></ref><ref id="B100"><label>100.</label><mixed-citation>100. Zorzini V., Buts L., Sleutel M., Garcia-Pino A., Talavera A. Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics. Nucleic Acids Research, 2014, vol. 42, no. 10, pp. 6709–6725.</mixed-citation></ref></ref-list></back></article>
