Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA

mBio

Volumn 5, Issue 1, 2014, Pages

  Lebreton, Alice ^a,b,c   Job, Viviana ^d,e,f   Ragon, Marie ^a   Le Monnier, Alban ^a,h,i   Dessen, Andréa ^d,e,f,g   Cossart, Pascale ^a,b,c   Bierne, Hélène ^a,b,c,j  

^a INSTITUT PASTEUR   (France)

^b INSERM   (France)

^c CEMAGREF   (France)

^d UNIV GRENOBLE ALPES   (France)

^e DIF   (France)

^f CNRS   (France)

^g BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

^h University Paris Sud   (France)

ⁱ SAINT JOSEPH HOSPITAL   (France)

^j UMR1319 MICALIS   (France)

more..

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN BAHD1; PROTEIN LNTA; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; IN VITRO STUDY; LISTERIA MONOCYTOGENES; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN MOTIF; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA EXTRACTION; SEROTYPE;

CELL LINE; CHROMOSOMAL PROTEINS, NON-HISTONE; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; HUMANS; INTERFERONS; LISTERIA MONOCYTOGENES; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; VIRULENCE FACTORS;

EID: 84903363844     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00775-13     Document Type: Article

References (29)

1. Allerberger F, Wagner M. 2010. Listeriosis: a resurgent foodborne infection. Clin. Microbiol. Infect. 16:16-23. http://dx.doi.org/10.1111/j.1469-0691.2009.03109.x.
2. Stavru F, Archambaud C, Cossart P. 2011. Cell biology and immunology of Listeria monocytogenes infections: novel insights. Immunol. Rev. 240: 160-184. http://dx.doi.org/10.1111/j.1600-065X.2010.00993.x.
3. Zenewicz LA, Shen H. 2007. Innate and adaptive immune responses to Listeria monocytogenes: a short overview. Microbes Infect. 9:1208-1215. http://dx.doi.org/10.1016/j.micinf.2007.05.008.
4. Camejo A, Carvalho F, Reis O, Leitão E, Sousa S, Cabanes D. 2011. The arsenal of virulence factors deployed by Listeria monocytogenes to promote its cell infection cycle. Virulence 2:379-394. http://dx.doi.org/10.4161/ viru.2.5.17703.
5. Cossart P. 2011. Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes. Proc. Natl. Acad. Sci. U. S. A. 108:19484-19491. http://dx.doi.org/10.1073/pnas.1112371108.
6. Freitag NE, Port GC, Miner MD. 2009. Listeria monocytogenes-from saprophyte to intracellular pathogen. Nat. Rev. Microbiol. 7:623-628. http://dx.doi.org/10.1038/nrmicro2171.
7. Bierne H, Cossart P. 2002. InlB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor. J. Cell Sci. 115: 3357-3367.
8. Gouin E, Adib-Conquy M, Balestrino D, Nahori MA, Villiers V, Colland F, Dramsi S, Dussurget O, Cossart P. 2010. The Listeria monocytogenes InlC protein interferes with innate immune responses by targeting the IκB kinase subunit IKKα. Proc. Natl. Acad. Sci. U. S. A. 107: 17333-17338. http://dx.doi.org/10.1073/pnas.1007765107.
9. Hamon MA, Batsché E, Régnault B, Tham TN, Seveau S, Muchardt C, Cossart P. 2007. Histone modifications induced by a family of bacterial toxins. Proc. Natl. Acad. Sci. U. S. A. 104:13467-13472. http://dx.doi.org/ 10.1073/pnas.0702729104.
10. Lebreton A, Lakisic G, Job V, Fritsch L, Tham TN, Camejo A, Matteï PJ, Regnault B, Nahori MA, Cabanes D, Gautreau A, Ait-Si-Ali S, Dessen A, Cossart P, Bierne H. 2011. A bacterial protein targets the BAHD1 chromatin complex to stimulate type III interferon response. Science 331: 1319-1321. http://dx.doi.org/10.1126/science.1200120.
11. Hamon MA, Cossart P. 2011. K+ efflux is required for histone H3 dephosphorylation by Listeria monocytogenes listeriolysin O and other pore-forming toxins. Infect. Immun. 79:2839-2846. http://dx.doi.org/ 10.1128/IAI.01243-10.
12. Lebreton A, Cossart P, Bierne H. 2012. Bacteria tune interferon responses by playing with chromatin. Virulence 3:87-91. http://dx.doi.org/ 10.4161/viru.3.1.18531.
13. Bierne H, Hamon M, Cossart P. 2012. Epigenetics and bacterial infections. Cold Spring Harb Perspect. Med 2:a010272. http://dx.doi.org/ 10.1101/cshperspect.a010272.
14. Bierne H, Cossart P. 2012. When bacteria target the nucleus: the emerging family of nucleomodulins. Cell. Microbiol. 14:622-633. http:// dx.doi.org/10.1111/j.1462-5822.2012.01758.x.
15. Bierne H, Tham TN, Batsche E, Dumay A, Leguillou M, Kernéis-Golsteyn S, Regnault B, Seeler JS, Muchardt C, Feunteun J, Cossart P. 2009. Human BAHD1 promotes heterochromatic gene silencing. Proc. Natl. Acad. Sci. U. S. A. 106:13826-13831. http://dx.doi.org/10.1073/ pnas.0901259106.
16. Yang N, Xu RM. 2013. Structure and function of the BAH domain in chromatin biology. Crit. Rev. Biochem. Mol. Biol. 48:211-221. http:// dx.doi.org/10.3109/10409238.2012.742035.
17. Barandun J, Delley CL, Weber-Ban E. 2012. The pupylation pathway and its role in mycobacteria. BMC Biol. 10:95. http://dx.doi.org/10.1186/ 1741-7007-10-95.
18. Jones JD, O'Connor CD. 2011. Protein acetylation in prokaryotes. Proteomics 11:3012-3022. http://dx.doi.org/10.1002/pmic.201000812.
19. Ragon M, Wirth T, Hollandt F, Lavenir R, Lecuit M, Le Monnier A, Brisse S. 2008. A new perspective on Listeria monocytogenes evolution. PLoS Pathog. 4:e1000146. http://dx.doi.org/10.1371/ journal.ppat.1000146.
20. den Bakker HC, Cummings CA, Ferreira V, Vatta P, Orsi RH, Degoricija L, Barker M, Petrauskene O, Furtado MR, Wiedmann M. 2010. Comparative genomics of the bacterial genus Listeria: genome evolution is characterized by limited gene acquisition and limited gene loss. BMC Genomics 11:688. http://dx.doi.org/10.1186/1471-2164-11-688.
21. Kay BK, Williamson MP, Sudol M. 2000. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14:231-241.
22. Kuenne C, Billion A, Mraheil MA, Strittmatter A, Daniel R, Goesmann A, Barbuddhe S, Hain T, Chakraborty T. 2013. Reassessment of the Listeria monocytogenes pan-genome reveals dynamic integration hotspots and mobile genetic elements as major components of the accessory genome. BMC Genomics 14:47. http://dx.doi.org/10.1186/1471-2164-14-47.
23. Jonquières R, Bierne H, Mengaud J, Cossart P. 1998. The inlA gene of Listeria monocytogenes LO28 harbors a nonsense mutation resulting in release of internalin. Infect. Immun. 66:3420-3422.
24. Jacquet C, Doumith M, Gordon JI, Martin PM, Cossart P, Lecuit M. 2004. A molecular marker for evaluating the pathogenic potential of foodborne Listeria monocytogenes. J. Infect. Dis. 189:2094-2100. http:// dx.doi.org/10.1086/420853.
25. den Bakker HC, Wiedmann M. 16 May 2011. New Listeria virulence gene also found in a non-pathogenic Listeria species. Science. http:// www. science mag. org/content/331/6022/1319. abstract/ reply#sci_el_14407.
26. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ. 2007. Phaser crystallographic software. J. Appl. Crystallogr. 40: 658-674. http://dx.doi.org/10.1107/S0021889807021206.
27. Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. http:// dx.doi.org/10.1107/S0907444904019158.
28. Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53:240-255. http://dx.doi.org/10.1107/ S0907444996012255.
29. Fritsch L, Robin P, Mathieu JR, Souidi M, Hinaux H, Rougeulle C, Harel-Bellan A, Ameyar-Zazoua M, Ait-Si-Ali S. 2010. A subset of the histone H3 lysine 9 methyltransferases Suv39h1, G9a, GLP, and SETDB1 participate in a multimeric complex. Mol. Cell 37:46-56. http:// dx.doi.org/10.1016/j.molcel.2009.12.017.