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O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity

Bibliographic reference Rolain, Thomas ; Bernard, Elvis ; Beaussart, Audrey ; Degand, Hervé ; courtin, Pascal ; et. al. O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity. In: Journal of Biological Chemistry, Vol. 288, no. 31, p. 22233-22247 (2013)
Permanent URL http://hdl.handle.net/2078.1/130128
  1. Xu Qingping, Sudek Sebastian, McMullan Daniel, Miller Mitchell D., Geierstanger Bernhard, Jones David H., Krishna S. Sri, Spraggon Glen, Bursalay Badry, Abdubek Polat, Acosta Claire, Ambing Eileen, Astakhova Tamara, Axelrod Herbert L., Carlton Dennis, Caruthers Jonathan, Chiu Hsiu-Ju, Clayton Thomas, Deller Marc C., Duan Lian, Elias Ylva, Elsliger Marc-André, Feuerhelm Julie, Grzechnik Slawomir K., Hale Joanna, Won Han Gye, Haugen Justin, Jaroszewski Lukasz, Jin Kevin K., Klock Heath E., Knuth Mark W., Kozbial Piotr, Kumar Abhinav, Marciano David, Morse Andrew T., Nigoghossian Edward, Okach Linda, Oommachen Silvya, Paulsen Jessica, Reyes Ron, Rife Christopher L., Trout Christina V., van den Bedem Henry, Weekes Dana, White Aprilfawn, Wolf Guenter, Zubieta Chloe, Hodgson Keith O., Wooley John, Deacon Ashley M., Godzik Adam, Lesley Scott A., Wilson Ian A., Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase, 10.1016/j.str.2008.12.008
  2. Bernard Elvis, Rolain Thomas, Courtin Pascal, Guillot Alain, Langella Philippe, Hols Pascal, Chapot-Chartier Marie-Pierre, Characterization ofO-Acetylation ofN-Acetylglucosamine : A NOVEL STRUCTURAL VARIATION OF BACTERIAL PEPTIDOGLYCAN, 10.1074/jbc.m111.241414
  3. Xu Qingping, Abdubek Polat, Astakhova Tamara, Axelrod Herbert L., Bakolitsa Constantina, Cai Xiaohui, Carlton Dennis, Chen Connie, Chiu Hsiu-Ju, Chiu Michelle, Clayton Thomas, Das Debanu, Deller Marc C., Duan Lian, Ellrott Kyle, Farr Carol L., Feuerhelm Julie, Grant Joanna C., Grzechnik Anna, Han Gye Won, Jaroszewski Lukasz, Jin Kevin K., Klock Heath E., Knuth Mark W., Kozbial Piotr, Krishna S. Sri, Kumar Abhinav, Lam Winnie W., Marciano David, Miller Mitchell D., Morse Andrew T., Nigoghossian Edward, Nopakun Amanda, Okach Linda, Puckett Christina, Reyes Ron, Tien Henry J., Trame Christine B., van den Bedem Henry, Weekes Dana, Wooten Tiffany, Yeh Andrew, Hodgson Keith O., Wooley John, Elsliger Marc-André, Deacon Ashley M., Godzik Adam, Lesley Scott A., Wilson Ian A., Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC fromBacillus cereusin complex withL-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases, 10.1107/s1744309110021214
  4. Claes Ingmar J. J., Schoofs Geert, Regulski Krzysztof, Courtin Pascal, Chapot-Chartier Marie-Pierre, Rolain Thomas, Hols Pascal, von Ossowski Ingemar, Reunanen Justus, de Vos Willem M., Palva Airi, Vanderleyden Jos, De Keersmaecker Sigrid C. J., Lebeer Sarah, Genetic and Biochemical Characterization of the Cell Wall Hydrolase Activity of the Major Secreted Protein of Lactobacillus rhamnosus GG, 10.1371/journal.pone.0031588
  5. Eckert C., Lecerf M., Dubost L., Arthur M., Mesnage S., Functional Analysis of AtlA, the Major N-Acetylglucosaminidase of Enterococcus faecalis, 10.1128/jb.01145-06
  6. Huard C., Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis, 10.1099/mic.0.25875-0
  7. Regulski Krzysztof, Courtin Pascal, Meyrand Mickael, Claes Ingmar J. J., Lebeer Sarah, Vanderleyden Jos, Hols Pascal, Guillot Alain, Chapot-Chartier Marie-Pierre, Analysis of the Peptidoglycan Hydrolase Complement of Lactobacillus casei and Characterization of the Major γ-D-Glutamyl-L-Lysyl-Endopeptidase, 10.1371/journal.pone.0032301
  8. Lebeer Sarah, Claes Ingmar JJ, Balog Crina IA, Schoofs Geert, Verhoeven Tine LA, Nys Kris, von Ossowski Ingemar, de Vos Willem M, Tytgat Hanne LP, Agostinis Patrizia, Palva Airi, Van Damme Els JM, Deelder André M, De Keersmaecker Sigrid CJ, Wuhrer Manfred, Vanderleyden Jos, The major secreted protein Msp1/p75 is O-glycosylated in Lactobacillus rhamnosus GG, 10.1186/1475-2859-11-15
  9. Otzen Daniel, N for AsN - O for StrOcture? A strand-loop-strand motif for prokaryotic O-glycosylation : A structural motif for prokaryotic O-glycosylation, 10.1111/j.1365-2958.2012.07972.x
  10. Nothaft Harald, Szymanski Christine M., Protein glycosylation in bacteria: sweeter than ever, 10.1038/nrmicro2383
  11. Zarschler K., Janesch B., Pabst M., Altmann F., Messner P., Schaffer C., Protein tyrosine O-glycosylation--A rather unexplored prokaryotic glycosylation system, 10.1093/glycob/cwq035
  12. Vollmer Waldemar, Blanot Didier, De Pedro Miguel A., Peptidoglycan structure and architecture, 10.1111/j.1574-6976.2007.00094.x
  13. Vik Åshild, Aspholm Marina, Anonsen Jan Haug, Børud Bente, Roos Norbert, Koomey Michael, Insights into type IV pilus biogenesis and dynamics from genetic analysis of a C-terminally tagged pilin: a role forO-linked glycosylation : Pilin glycosylation affects type IV pilus dynamics, 10.1111/j.1365-2958.2012.08166.x
  14. Vik A., Aas F. E., Anonsen J. H., Bilsborough S., Schneider A., Egge-Jacobsen W., Koomey M., Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae, 10.1073/pnas.0809504106
  15. Kawamura, J. Biol. Chem, 258, 9514 (1983)
  16. Moens Sara, Vanderleyden J., Glycoproteins in prokaryotes, 10.1007/s002030050484
  17. Webster, Appl. Environ. Microbiol, 41, 371 (1981)
  18. Sambrook J. Fritsch E. Maniatis T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
  19. Holo, Appl. Environ. Microbiol, 55, 3119 (1989)
  20. Pavan S., Hols P., Delcour J., Geoffroy M.-C., Grangette C., Kleerebezem M., Mercenier A., Adaptation of the Nisin-Controlled Expression System in Lactobacillus plantarum: a Tool To Study In Vivo Biological Effects, 10.1128/aem.66.10.4427-4432.2000
  21. de Ruyter, Appl. Environ. Microbiol, 62, 3662 (1996)
  22. Kuipers Oscar P., de Ruyter Pascalle G.G.A., Kleerebezem Michiel, de Vos Willem M., Controlled overproduction of proteins by lactic acid bacteria, 10.1016/s0167-7799(97)01029-9
  23. Courtin P., Miranda G., Guillot A., Wessner F., Mezange C., Domakova E., Kulakauskas S., Chapot-Chartier M.-P., Peptidoglycan Structure Analysis of Lactococcus lactis Reveals the Presence of an L,D-Carboxypeptidase Involved in Peptidoglycan Maturation, 10.1128/jb.00285-06
  24. Vollmer Waldemar, Joris Bernard, Charlier Paulette, Foster Simon, Bacterial peptidoglycan (murein) hydrolases, 10.1111/j.1574-6976.2007.00099.x
  25. Cornett, J. Bacteriol, 135, 153 (1978)
  26. Wessel D., Flügge U.I., A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids, 10.1016/0003-2697(84)90782-6
  27. Andre G., Leenhouts K., Hols P., Dufrene Y. F., Detection and Localization of Single LysM-Peptidoglycan Interactions, 10.1128/jb.00519-08
  28. Hinterdorfer Peter, Dufrêne Yves F, Detection and localization of single molecular recognition events using atomic force microscopy, 10.1038/nmeth871
  29. Francius Grégory, Alsteens David, Dupres Vincent, Lebeer Sarah, De Keersmaecker Sigrid, Vanderleyden Jos, Gruber Hermann J, Dufrêne Yves F, Stretching polysaccharides on live cells using single molecule force spectroscopy, 10.1038/nprot.2009.65
  30. Cheng Qi, Fischetti Vincent A., Mutagenesis of a bacteriophage lytic enzyme PlyGBS significantly increases its antibacterial activity against group B streptococci, 10.1007/s00253-006-0771-1
  31. Eldholm Vegard, Johnsborg Ola, Straume Daniel, Ohnstad Hilde Solheim, Berg Kari Helene, Hermoso Juan A., Håvarstein Leiv Sigve, Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide : The pneumococcal murein hydrolase CbpD, 10.1111/j.1365-2958.2010.07143.x
  32. Layec Séverine, Gérard Joëlle, Legué Valérie, Chapot-Chartier Marie-Pierre, Courtin Pascal, Borges Frédéric, Decaris Bernard, Leblond-Bourget Nathalie, The CHAP domain of Cse functions as an endopeptidase that acts at mature septa to promoteStreptococcus thermophiluscell separation, 10.1111/j.1365-2958.2009.06595.x
  33. Low Lieh Yoon, Yang Chen, Perego Marta, Osterman Andrei, Liddington Robert C., Structure and Lytic Activity of aBacillus anthracisProphage Endolysin, 10.1074/jbc.m502723200
  34. Rodriguez-Rubio L., Martinez B., Rodriguez A., Donovan D. M., Garcia P., Enhanced Staphylolytic Activity of the Staphylococcus aureus Bacteriophage vB_SauS-phiIPLA88 HydH5 Virion-Associated Peptidoglycan Hydrolase: Fusions, Deletions, and Synergy with LysH5, 10.1128/aem.07621-11
  35. Rolain Thomas, Bernard Elvis, Courtin Pascal, Bron Peter A, Kleerebezem Michiel, Chapot-Chartier Marie-Pierre, Hols Pascal, Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1, 10.1186/1475-2859-11-137
  36. Eugster M. R., Loessner M. J., Wall Teichoic Acids Restrict Access of Bacteriophage Endolysin Ply118, Ply511, and PlyP40 Cell Wall Binding Domains to the Listeria monocytogenes Peptidoglycan, 10.1128/jb.00808-12
  37. Fukushima T., Afkham A., Kurosawa S.-i., Tanabe T., Yamamoto H., Sekiguchi J., A New D,L-Endopeptidase Gene Product, YojL (Renamed CwlS), Plays a Role in Cell Separation with LytE and LytF in Bacillus subtilis, 10.1128/jb.00188-06
  38. Schlag Martin, Biswas Raja, Krismer Bernhard, Kohler Thomas, Zoll Sebastian, Yu Wenqi, Schwarz Heinz, Peschel Andreas, Götz Friedrich, Role of staphylococcal wall teichoic acid in targeting the major autolysin Atl, 10.1111/j.1365-2958.2009.07007.x
  39. Steen Anton, Buist Girbe, Leenhouts Kees J., Khattabi Mohamed El, Grijpstra Froukje, Zomer Aldert L., Venema Gerard, Kuipers Oscar P., Kok Jan, Cell Wall Attachment of a Widely Distributed Peptidoglycan Binding Domain Is Hindered by Cell Wall Constituents, 10.1074/jbc.m211055200
  40. Yamamoto Hiroki, Miyake Yukiko, Hisaoka Miharu, Kurosawa Shin-ichirou, Sekiguchi Junichi, The major and minor wall teichoic acids prevent the sidewall localization of vegetative dl-endopeptidase LytF inBacillus subtilis, 10.1111/j.1365-2958.2008.06397.x
  41. Frankel Matthew B., Schneewind Olaf, Determinants of Murein Hydrolase Targeting to Cross-wall of Staphylococcus aureus Peptidoglycan , 10.1074/jbc.m111.336404
  42. Atilano M. L., Pereira P. M., Yates J., Reed P., Veiga H., Pinho M. G., Filipe S. R., Teichoic acids are temporal and spatial regulators of peptidoglycan cross-linking in Staphylococcus aureus, 10.1073/pnas.1004304107
  43. Charbonneau Marie-Ève, Côté Jean-Philippe, Haurat M. Florencia, Reiz Bela, Crépin Sébastien, Berthiaume Frédéric, Dozois Charles M., Feldman Mario F., Mourez Michael, A structural motif is the recognition site for a new family of bacterial protein O-glycosyltransferases : Substrate specificity of the Aah glycosyltransferase, 10.1111/j.1365-2958.2012.07973.x
  44. Fletcher C. Mark, Coyne Michael J., Villa Otto F., Chatzidaki-Livanis Maria, Comstock Laurie E., A General O-Glycosylation System Important to the Physiology of a Major Human Intestinal Symbiont, 10.1016/j.cell.2009.02.041
  45. Bublitz Maike, Polle Lilia, Holland Christin, Heinz Dirk W., Nimtz Manfred, Schubert Wolf-Dieter, Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase ofListeria monocytogenes, 10.1111/j.1365-2958.2009.06619.x
  46. Palumbo E., Deghorain M., Cocconcelli P. S., Kleerebezem M., Geyer A., Hartung T., Morath S., Hols P., D-Alanyl Ester Depletion of Teichoic Acids in Lactobacillus plantarum Results in a Major Modification of Lipoteichoic Acid Composition and Cell Wall Perforations at the Septum Mediated by the Acm2 Autolysin, 10.1128/jb.188.10.3709-3715.2006
  47. Odintsov Sergey G., Sabala Izabela, Marcyjaniak Malgorzata, Bochtler Matthias, Latent LytM at 1.3Å Resolution, 10.1016/j.jmb.2003.11.009
  48. Pérez-Dorado Inmaculada, González Ana, Morales María, Sanles Reyes, Striker Waldemar, Vollmer Waldemar, Mobashery Shahriar, García José L, Martínez-Ripoll Martín, García Pedro, Hermoso Juan A, Insights into pneumococcal fratricide from the crystal structures of the modular killing factor LytC, 10.1038/nsmb.1817
  49. Ruggiero Alessia, Marasco Daniela, Squeglia Flavia, Soldini Silvia, Pedone Emilia, Pedone Carlo, Berisio Rita, Structure and Functional Regulation of RipA, a Mycobacterial Enzyme Essential for Daughter Cell Separation, 10.1016/j.str.2010.06.007
  50. Yang Desirée C., Tan Kemin, Joachimiak Andrzej, Bernhardt Thomas G., A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division : Control of cell wall-remodelling enzymes, 10.1111/j.1365-2958.2012.08138.x
  51. Serrano L. Mariela, Molenaar Douwe, Wels Michiel, Teusink Bas, Bron Peter A., de Vos Willem M., Smid Eddy J., Thioredoxin reductase is a key factor in the oxidative stress response of Lactobacillus plantarum WCFS1, 10.1186/1475-2859-6-29
  52. Bradford Marion M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, 10.1016/0003-2697(76)90527-3
  53. Cantarel B. L., Coutinho P. M., Rancurel C., Bernard T., Lombard V., Henrissat B., The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics, 10.1093/nar/gkn663
  54. Fredriksen L., Mathiesen G., Moen A., Bron P. A., Kleerebezem M., Eijsink V. G. H., Egge-Jacobsen W., The Major Autolysin Acm2 from Lactobacillus plantarum Undergoes Cytoplasmic O-Glycosylation, 10.1128/jb.06314-11
  55. Kleerebezem Michiel, Hols Pascal, Bernard Elvis, Rolain Thomas, Zhou Miaomiao, Siezen Roland J., Bron Peter A., The extracellular biology of the lactobacilli, 10.1111/j.1574-6976.2009.00208.x
  56. Lu Jeff Zhiqiang, Fujiwara Tamaki, Komatsuzawa Hitoshi, Sugai Motoyuki, Sakon Joshua, Cell Wall-targeting Domain of Glycylglycine Endopeptidase Distinguishes among Peptidoglycan Cross-bridges, 10.1074/jbc.m509691200