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[[File:Transfection_by_Agrobacterium.svg|thumb|330x330px|''[[Agrobacterium tumefaciens]]'' (A) targets the nucleus of a plant cell (D) during an infection.]]

'''Nucleomodulins''' are a family of bacterial proteins that enter the nucleus of [[Eukaryotic Cells|eukaryotic cells]].<ref name=":2">{{Cite journal|last1=Bierne|first1=Hélène|last2=Cossart|first2=Pascale|date=May 2012|title=When bacteria target the nucleus: the emerging family of nucleomodulins|journal=Cellular Microbiology|volume=14|issue=5|pages=622–33|doi=10.1111/j.1462-5822.2012.01758.x|issn=1462-5822|pmid=22289128|s2cid=40506912|doi-access=free}}</ref>

This term comes from the contraction between "nucleus" and "modulins", which are microbial molecules that modulate the behaviour of eukaryotic cells. Nucleomodulins are produced by pathogenic or symbiotic bacteria. They act on various processes in the [[Cell nucleus|nucleus]]: remodelling of the [[chromatin]] structure,<ref>{{Cite journal|last1=Skrzypek|first1=E.|last2=Cowan|first2=C.|last3=Straley|first3=S. C.|date=December 1998|title=Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus|journal=Molecular Microbiology|volume=30|issue=5|pages=1051–65|doi=10.1046/j.1365-2958.1998.01135.x|issn=0950-382X|pmid=9988481|s2cid=5562445|doi-access=free}}</ref><ref>{{Cite journal|last1=Li|first1=Hongtao|last2=Xu|first2=Hao|last3=Zhou|first3=Yan|last4=Zhang|first4=Jie|date=2007-02-16|title=The phosphothreonine lyase activity of a bacterial type III effector family|journal=Science|volume=315|issue=5814|pages=1000–3|doi=10.1126/science.1138960|issn=1095-9203|pmid=17303758|bibcode=2007Sci...315.1000L|s2cid=6798326}}</ref><ref>{{Cite journal|last1=Arbibe|first1=Laurence|last2=Kim|first2=Dong Wook|last3=Batsche|first3=Eric|last4=Pedron|first4=Thierry|date=January 2007|title=An injected bacterial effector targets chromatin access for transcription factor NF-kappaB to alter transcription of host genes involved in immune responses|journal=Nature Immunology|volume=8|issue=1|pages=47–56|doi=10.1038/ni1423|issn=1529-2908|pmid=17159983|s2cid=25557624}}</ref><ref>{{Cite journal|last1=Pennini|first1=Meghan E.|last2=Perrinet|first2=Stéphanie|last3=Dautry-Varsat|first3=Alice|last4=Subtil|first4=Agathe|date=2010-07-15|title=Histone methylation by NUE, a novel nuclear effector of the intracellular pathogen Chlamydia trachomatis|journal=PLOS Pathogens|volume=6|issue=7|article-number=e1000995|doi=10.1371/journal.ppat.1000995|issn=1553-7374|pmc=2904774|pmid=20657819 |doi-access=free }}</ref><ref>{{Cite journal|last1=Rolando|first1=Monica|last2=Sanulli|first2=Serena|last3=Rusniok|first3=Christophe|last4=Gomez-Valero|first4=Laura|date=April 2013|title=Legionella pneumophila Effector RomA Uniquely Modifies Host Chromatin to Repress Gene Expression and Promote Intracellular Bacterial Replication|journal=Cell Host & Microbe|language=en|volume=13|issue=4|pages=395–405|doi=10.1016/j.chom.2013.03.004|pmid=23601102|doi-access=free}}</ref><ref>{{Cite journal|last1=Li|first1=Ting|last2=Lu|first2=Qiuhe|last3=Wang|first3=Guolun|last4=Xu|first4=Hao|date=August 2013|title=SET-domain bacterial effectors target heterochromatin protein 1 to activate host rDNA transcription|journal=EMBO Reports|language=en|volume=14|issue=8|pages=733–40|doi=10.1038/embor.2013.86|issn=1469-221X|pmc=3736128|pmid=23797873}}</ref><ref name=":0">{{Cite journal|last1=Lebreton|first1=Alice|last2=Lakisic|first2=Goran|last3=Job|first3=Viviana|last4=Fritsch|first4=Lauriane|date=2011-03-11|title=A bacterial protein targets the BAHD1 chromatin complex to stimulate type III interferon response|journal=Science|volume=331|issue=6022|pages=1319–21|doi=10.1126/science.1200120|issn=1095-9203|pmid=21252314|bibcode=2011Sci...331.1319L|s2cid=35405265|url=https://hal-cea.archives-ouvertes.fr/cea-00819299/file/Science_2011_post-print.pdf }}</ref><ref>{{Cite journal|last1=Rennoll-Bankert|first1=Kristen E.|last2=Garcia-Garcia|first2=Jose C.|last3=Sinclair|first3=Sara H.|last4=Dumler|first4=J. Stephen|date=November 2015|title=Chromatin-bound bacterial effector ankyrin A recruits histone deacetylase 1 and modifies host gene expression: AnkA recruits HDAC1 to modify CYBB expression|journal=Cellular Microbiology|language=en|volume=17|issue=11|pages=1640–52|doi=10.1111/cmi.12461|pmc=5845759|pmid=25996657}}</ref><ref>{{Cite journal|last1=Farris|first1=Tierra R.|last2=Dunphy|first2=Paige S.|last3=Zhu|first3=Bing|last4=Kibler|first4=Clayton E.|date=November 2016|title=Ehrlichia chaffeensis TRP32 Is a Nucleomodulin That Directly Regulates Expression of Host Genes Governing Differentiation and Proliferation|journal=Infection and Immunity|language=en|volume=84|issue=11|pages=3182–3194|doi=10.1128/IAI.00657-16|issn=0019-9567|pmc=5067751|pmid=27572329}}</ref><ref>{{Cite journal|last1=Mitra|first1=Shubhajit|last2=Dunphy|first2=Paige S.|last3=Das|first3=Seema|last4=Zhu|first4=Bing|date=2018-01-22|title=Ehrlichia chaffeensis TRP120 Effector Targets and Recruits Host Polycomb Group Proteins for Degradation To Promote Intracellular Infection|journal=Infection and Immunity|language=en|volume=86|issue=4|page=e00845–17, /iai/86/4/e00845–17.atom|doi=10.1128/IAI.00845-17|issn=0019-9567|pmc=5865042|pmid=29358333}}</ref><ref>{{Cite journal|last1=Yaseen|first1=Imtiyaz|last2=Kaur|first2=Prabhjot|last3=Nandicoori|first3=Vinay Kumar|last4=Khosla|first4=Sanjeev|date=December 2015|title=Mycobacteria modulate host epigenetic machinery by Rv1988 methylation of a non-tail arginine of histone H3|journal=Nature Communications|language=en|volume=6|issue=1|page=8922|doi=10.1038/ncomms9922|pmid=26568365|bibcode=2015NatCo...6.8922Y|issn=2041-1723|doi-access=free}}</ref>{{citation overkill|date=April 2020}} [[Transcription (biology)|transcription]],<ref>{{Cite journal|last1=Kay|first1=Sabine|last2=Hahn|first2=Simone|last3=Marois|first3=Eric|last4=Hause|first4=Gerd|date=2007-10-26|title=A Bacterial Effector Acts as a Plant Transcription Factor and Induces a Cell Size Regulator|journal=Science|language=en|volume=318|issue=5850|pages=648–651|doi=10.1126/science.1144956|pmid=17962565|bibcode=2007Sci...318..648K|s2cid=11544887|issn=0036-8075}}</ref><ref>{{Cite journal|last1=Römer|first1=Patrick|last2=Hahn|first2=Simone|last3=Jordan|first3=Tina|last4=Strauß|first4=Tina|date=2007-10-26|title=Plant Pathogen Recognition Mediated by Promoter Activation of the Pepper Bs3 Resistance Gene|journal=Science|language=en|volume=318|issue=5850|pages=645–8|doi=10.1126/science.1144958|pmid=17962564|bibcode=2007Sci...318..645R|s2cid=19340482|issn=0036-8075}}</ref> [[RNA splicing|splicing of pre-messenger RNA]],<ref>{{Cite journal|last1=Toyotome|first1=Takahito|last2=Suzuki|first2=Toshihiko|last3=Kuwae|first3=Asaomi|last4=Nonaka|first4=Takashi|date=2001-08-24|title=Shigella Protein IpaH 9.8 Is Secreted from Bacteria within Mammalian Cells and Transported to the Nucleus|journal=Journal of Biological Chemistry|language=en|volume=276|issue=34|pages=32071–32079|doi=10.1074/jbc.M101882200|pmid=11418613|issn=0021-9258|doi-access=free}}</ref><ref name=":1">{{Cite journal|last1=Okuda|first1=Jun|last2=Toyotome|first2=Takahito|last3=Kataoka|first3=Naoyuki|last4=Ohno|first4=Mutsuhito|date=July 2005|title=Shigella effector IpaH9.8 binds to a splicing factor U2AF35 to modulate host immune responses|journal=Biochemical and Biophysical Research Communications|language=en|volume=333|issue=2|pages=531–9|doi=10.1016/j.bbrc.2005.05.145|pmid=15950937}}</ref> [[cell division]].<ref>{{Cite journal|last1=Taieb|first1=Frédéric|last2=Nougayrède|first2=Jean-Philippe|last3=Oswald|first3=Eric|date=2011-03-29|title=Cycle Inhibiting Factors (Cifs): Cyclomodulins That Usurp the Ubiquitin-Dependent Degradation Pathway of Host Cells|journal=Toxins|language=en|volume=3|issue=4|pages=356–68|doi=10.3390/toxins3040356|issn=2072-6651|pmc=3202828|pmid=22069713|doi-access=free}}</ref>

The identification of nucleomodulins in several species of bacterial pathogens of humans, animals and plants has led to the emergence of the concept that direct control of the nucleus is one of the most sophisticated strategies used by microbes to bypass host defences. Nucleomodulins can be directly secreted into the intracellular medium after entry of the bacteria into the cell, like ''[[Listeria monocytogenes]]'', or they can be injected from the extracellular medium or intracellular [[organelle]]s using a type [[Type three secretion system|III]] or [[Type IV secretion system|IV]] bacterial secretion system, also known as a "molecular syringe".{{citation needed|date=April 2020}}

More recently, it has been shown that some of them, such as YopM from ''[[Yersinia pestis]]'' and IpaH9.8 from ''[[Shigella flexneri]]'', can autonomously penetrate eukaryotic cells thanks to a membrane transduction domain.<ref>{{Cite journal|last1=Norkowski|first1=Stefanie|last2=Körner|first2=Britta|last3=Greune|first3=Lilo|last4=Stolle|first4=Anne-Sophie|last5=Lubos|first5=Marie-Luise|last6=Hardwidge|first6=Philip R.|last7=Schmidt|first7=M. Alexander|last8=Rüter|first8=Christian|date=2018-06-01|title=Bacterial LPX motif-harboring virulence factors constitute a species-spanning family of cell-penetrating effectors|journal=Cellular and Molecular Life Sciences|language=en|volume=75|issue=12|pages=2273–2289|doi=10.1007/s00018-017-2733-4|pmid=29285573|s2cid=7904315|issn=1420-9071|pmc=11105228}}</ref>

The diversity of molecular mechanisms triggered by nucleomodulins <ref name=":2"/><ref>{{Citation|last=Bierne|first=Hélène|title=Epigenetics of Infectious Diseases|chapter=Cross Talk Between Bacteria and the Host Epigenetic Machinery|date=2017|pages=113–158|editor-last=Doerfler|editor-first=Walter|series=Epigenetics and Human Health|publisher=Springer International Publishing|language=en|doi=10.1007/978-3-319-55021-3_6|isbn=978-3-319-55021-3|editor2-last=Casadesús|editor2-first=Josep}}</ref> is a source of inspiration for new [[biotechnologies]]. They are true nano-machines capable of hijacking a multitude of nuclear processes. In research, nucleomodulins are the subject of in-depth studies that have led to the discovery of new human nuclear regulators, such as the [[Epigenetics|epigenetic]] regulator [[Bromo adjacent homology domain containing 1|BAHD1]].<ref name=":0"/>

== Examples ==
''[[Agrobacterium tumefaciens]]'', responsible for crown gall disease, produces an arsenal of Vir proteins, including VirD2 and VirE2, enabling the precise integration of a piece of its DNA, called [[T-DNA]], into that of the host plant <ref>{{Cite journal|last1=Pelczar|first1=Pawel|last2=Kalck|first2=Véronique|last3=Gomez|first3=Divina|last4=Hohn|first4=Barbara|date=June 2004|title=Agrobacterium proteins VirD2 and VirE2 mediate precise integration of synthetic T-DNA complexes in mammalian cells|journal=EMBO Reports|volume=5|issue=6|pages=632–7|doi=10.1038/sj.embor.7400165|issn=1469-221X|pmc=1299075|pmid=15153934}}</ref>

''[[Listeria monocytogenes]]'', responsible for listeriosis, can modulate the expression of immunity genes. One of the mechanisms at play involves the bacterial protein LntA, which inhibits the function of the epigenetic regulator BAHD1. The action of this nucleomodulin is associated with chromatin decompaction and activation of an interferon response genes.<ref name=":0"/><ref>{{Cite journal|last1=Lebreton|first1=Alice|last2=Job|first2=Viviana|last3=Ragon|first3=Marie|last4=Le Monnier|first4=Alban|date=2014-01-21|title=Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA|journal=mBio|volume=5|issue=1|pages=e00775-13|doi=10.1128/mBio.00775-13|issn=2150-7511|pmc=3903274|pmid=24449750}}</ref>

''[[Shigella flexneri]]'', responsible for shigellosis, secretes the IpaH9.8 protein targeting a [[mRNA]] splicing protein that disrupts the production of protein isoforms and the inflammatory response in humans.<ref name=":1"/>

[[Legionella pneumophila]], responsible for [[legionellosis]], secretes an [[enzyme]] with histone methyltransferase activity capable of methylating [[histone]]s at different [[chromosome]] loci <ref>{{Cite journal|last1=Rolando|first1=Monica|last2=Sanulli|first2=Serena|last3=Rusniok|first3=Christophe|last4=Gomez-Valero|first4=Laura|last5=Bertholet|first5=Clement|last6=Sahr|first6=Tobias|last7=Margueron|first7=Raphael|last8=Buchrieser|first8=Carmen|display-authors=1|date=April 2013|title=Legionella pneumophila Effector RomA Uniquely Modifies Host Chromatin to Repress Gene Expression and Promote Intracellular Bacterial Replication|journal=Cell Host & Microbe|language=en|volume=13|issue=4|pages=395–405|doi=10.1016/j.chom.2013.03.004|pmid=23601102|doi-access=free}}</ref> or at the level of [[ribosomal DNA]] (rDNA) in the nucleolus.<ref>{{Cite journal|last1=Li|first1=Ting|last2=Lu|first2=Qiuhe|last3=Wang|first3=Guolun|last4=Xu|first4=Hao|last5=Huang|first5=Huanwei|last6=Cai|first6=Tao|last7=Kan|first7=Biao|last8=Ge|first8=Jianning|last9=Shao|first9=Feng|display-authors=1|date=August 2013|title=SET-domain bacterial effectors target heterochromatin protein 1 to activate host rDNA transcription|journal=EMBO Reports|language=en|volume=14|issue=8|pages=733–740|doi=10.1038/embor.2013.86|issn=1469-221X|pmc=3736128|pmid=23797873}}</ref>

== References ==
<references />

[[Category:Genetics]]

Nucleomodulin - История изменений

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