Mutation of crp mediates Serratia marcescens serralysin and global secreted protein production

Research in Microbiology

Volumn 164, Issue 1, 2013, Pages 38-45

  Shanks, Robert M Q ^a   Stella, Nicholas A ^a   Arena, Kristin E ^a   Fender, James E ^a  

^a University of Pittsburgh School of Medicine   (United States)

Author keywords

Chitinase; Cyclic AMP; Flagella; Metalloprotease; Proteomics; Secretome

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CHITIN; CHITINASE; CRP PROTEIN; CYCLIC AMP; METALLOPROTEINASE; SERRALYSIN; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN SECRETION; PROTEIN SYNTHESIS; PROTEOMICS; RNA PURIFICATION; SERRATIA MARCESCENS; TYPE I SECRETION SYSTEM; WESTERN BLOTTING;

BACTERIAL PROTEINS; CYCLIC AMP; ENZYME ACTIVATION; LIPASE; MUTATION; PEPTIDE HYDROLASES; PROTEOME; SERRATIA MARCESCENS;

BACTERIA (MICROORGANISMS); SERRATIA MARCESCENS;

EID: 84871722859     PISSN: 09232508     EISSN: 17697123     Source Type: Journal    
DOI: 10.1016/j.resmic.2012.10.006     Document Type: Article

References (50)

1. Akatsuka H., Binet R., Kawai E., Wandersman C., Omori K. Lipase secretion by bacterial hybrid ATP-binding cassette exporters: molecular recognition of the LipBCD, PrtDEF, and HasDEF exporters. J. Bacteriol. 1997, 179:4754-4760.
2. Akatsuka H., Kawai E., Omori K., Shibatani T. The three genes lipB, lipC, and lipD involved in the extracellular secretion of the Serratia marcescens lipase which lacks an N-terminal signal peptide. J. Bacteriol. 1995, 177:6381-6389.
3. Akatsuka H., Kawai E., Sakurai N., Omori K. The Serratia marcescens bioH gene encodes an esterase. Gene 2003, 302:185-192.
4. Ball T.K., Wasmuth C.R., Braunagel S.C., Benedik M.J. Expression of Serratia marcescens extracellular proteins requires recA. J. Bacteriol. 1990, 172:342-349.
5. Basu B., Apte S.K. A novel serralysin metalloprotease from Deinococcus radiodurans. Biochim. Biophys. Acta 2008, 1784:1256-1264.
6. Benedik M.J., Strych U. Serratia marcescens and its extracellular nuclease. FEMS Microbiol. Lett. 1998, 165:1-13.
7. Binet R., Letoffe S., Ghigo J.M., Delepelaire P., Wandersman C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 1997, 192:7-11.
8. Brurberg M.B., Eijsink V.G., Haandrikman A.J., Venema G., Nes I.F. Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing. Microbiology 1995, 141:123-131.
9. Cruz-Romero M., Kelly A.L., Kerry J.P. Influence of packaging strategy on microbiological and biochemical changes in high-pressure-treated oysters. J. Sci. Food Agric. 2008, 88:2713-2723.
10. Felfoldi G., Marokhazi J., Kepiro M., Venekei I. Identification of natural target proteins indicates functions of a serralysin-type metalloprotease, PrtA, in anti-immune mechanisms. Appl. Environ. Microbiol. 2009, 75:3120-3126.
11. Fox A., Haas D., Reimmann C., Heeb S., Filloux A., Voulhoux R. Emergence of secretion-defective sublines of Pseudomonas aeruginosa PAO1 resulting from spontaneous mutations in the vfr global regulatory gene. Appl. Environ. Microbiol. 2008, 74:1902-1908.
12. Givskov M., Molin S. Expression of extracellular phospholipase from Serratia liquefaciens is growth-phase-dependent, catabolite-repressed and regulated by anaerobiosis. Mol. Microbiol. 1992, 6:1363-1374.
13. Givskov M., Molin S. Secretion of Serratia liquefaciens phospholipase from Escherichia coli. Mol. Microbiol. 1993, 8:229-242.
14. Green J., Scott C., Guest J.R. Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv. Microb. Physiol. 2001, 44:1-34.
15. Hejazi A., Falkiner F.R. Serratia marcescens. J. Med. Microbiol. 1997, 46:903-912.
16. Hertle R. The family of Serratia type pore forming toxins. Curr. Protein Pept. Sci. 2005, 6:313-325.
17. Heyduk T., Lee J.C. Escherichia coli cAMP receptor protein: evidence for three protein conformational states with different promoter binding affinities. Biochemistry 1989, 28:6914-6924.
18. Huang X.D., Yao K., Zhang H., Huang X.J., Xu Z.K. Surface modification of silicone intraocular lens by 2-methacryloyloxyethyl phosphoryl-choline binding to reduce Staphylococcus epidermidis adherence. Clin. Exp. Ophthalmol. 2007, 35:462-467.
19. Hume E.B., Willcox M.D. Emergence of Serratia marcescens as an ocular surface pathogen. Arch. Soc. Esp. Oftalmol. 2004, 79:475-477.
20. Hume E.B., Conerly L.L., Moreau J.M., Cannon B.M., Engel L.S., Stroman D.W., Hill J.M., O'callaghan R.J. Serratia marcescens keratitis: strain-specific corneal pathogenesis in rabbits. Curr. Eye Res. 1999, 19:525-532.
21. Ishizuka H., Hanamura A., Kunimura T., Aiba H. A lowered concentration of cAMP receptor protein caused by glucose is an important determinant for catabolite repression in Escherichia coli. Mol. Microbiol. 1993, 10:341-350.
22. Kalivoda E.J., Stella N.A., Aston M.A., Fender J.E., Thompson P.P., Kowalski R.P., Shanks R.M. Cyclic AMP negatively regulates prodigiosin production by Serratia marcescens. Res. Microbiol. 2010, 161:158-167.
23. Kalivoda E.J., Stella N.A., O'dee D.M., Nau G.J., Shanks R.M. The cyclic AMP-dependent catabolite repression system of Serratia marcescens mediates biofilm formation through regulation of type 1 fimbriae. Appl. Environ. Microbiol. 2008, 74:3461-3470.
24. Kamata R., Matsumoto K., Okamura R., Yamamoto T., Maeda H. The serratial 56K protease as a major pathogenic factor in serratial keratitis. Clinical and experimental study. Ophthalmology 1985, 92:1452-1459.
25. Kulasekara H.D., Ventre I., Kulasekara B.R., Lazdunski A., Filloux A., Lory S. A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol. Microbiol. 2005, 55:368-380.
26. Kumeta H., Hoshino T., Goda T., Okayama T., Shimada T., Ohgiya S., Matsuyama H., Ishizaki K. Identification of a member of the serralysin family isolated from a psychrotrophic bacterium, Pseudomonas fluorescens 114. Biosci. Biotechnol. Biochem. 1999, 63:1165-1170.
27. Letoffe S., Delepelaire P., Wandersman C. Cloning and expression in Escherichia coli of the Serratia marcescens metalloprotease gene: secretion of the protease from E. coli in the presence of the Erwinia chrysanthemi protease secretion functions. J. Bacteriol. 1991, 173:2160-2166.
28. Lin C.S., Horng J.T., Yang C.H., Tsai Y.H., Su L.H., Wei C.F., Chen C.C., Hsieh S.C., Lu C.C., Lai H.C. RssAB-FlhDC-ShlBA as a major pathogenesis pathway in Serratia marcescens. Infect. Immun. 2010, 78:4870-4881.
29. Louis D., Bernillon J., Wallach J.M. Specificity of Pseudomonas aeruginosa serralysin revisited, using biologically active peptides as substrates. Biochim. Biophys. Acta 1998, 1387:378-386.
30. Maeda H., Morihara K. Serralysin and related bacterial proteinases. Methods Enzymol. 1995, 248:395-413.
31. Marokhazi J., Mihala N., Hudecz F., Fodor A., Graf L., Venekei I. Cleavage site analysis of a serralysin-like protease, PrtA, from an insect pathogen Photorhabdus luminescens and development of a highly sensitive and specific substrate. FEBS J. 2007, 274:1946-1956.
32. Martìnez-Cadena M.G., Guzman-Verduzco L.M., Steieglitz H., Kupersztoch-Portnoy Y.M. Catabolite repression of Escherichia coli heat-stable enterotoxin activity. J. Bacteriol. 1981, 145:722-728.
33. Marty K.B., Williams C.L., Guynn L.J., Benedik M.J., Blanke S.R. Characterization of a cytotoxic factor in culture filtrates of Serratia marcescens. Infect. Immun. 2002, 70:1121-1128.
34. Massaoud M.K., Marokhazi J., Venekei I. Enzymatic characterization of a serralysin-like metalloprotease from the entomopathogen bacterium, Xenorhabdus. Biochim. Biophys. Acta 2011, 1814:1333-1339.
35. Matsumoto K. Role of bacterial proteases in pseudomonal and serratial keratitis. Biol. Chem. 2004, 385:1007-1016.
36. Matsumoto K., Maeda H., Takata K., Kamata R., Okamura R. Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958. J. Bacteriol. 1984, 157:225-232.
37. Matsumoto H., Noguchi H., Hayakawa Y. Primary cause of mortality in the armyworm larvae simultaneously parasitized by parasitic wasp and infected with bacteria. Eur. J. Biochem. 1998, 252:299-304.
38. Murdoch S.L., Trunk K., English G., Fritsch M.J., Pourkarimi E., Coulthurst S.J. The opportunistic pathogen Serratia marcescens utilizes type VI secretion to target bacterial competitors. J. Bacteriol. 2011, 193:6057-6069.
39. Rao V.A., Shepherd S.M., English G., Coulthurst S.J., Hunter W.N. The structure of Serratia marcescens Lip, a membrane-bound component of the type VI secretion system. Acta Crystallogr. D. Biol. Crystallogr. 2011, 67:1065-1072.
40. Reverchon S., Huang Y., Bourson C., Robert-Baudouy J. Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product. Gene 1989, 85:125-134.
41. Sapriel G., Wandersman C., Delepelaire P. The SecB chaperone is bifunctional in Serratia marcescens: SecB is involved in the Sec pathway and required for HasA secretion by the ABC transporter. J. Bacteriol. 2003, 185:80-88.
42. Shanks R.M., Dashiff A., Alster J.S., Kadouri D.E. Isolation and identification of a bacteriocin with antibacterial and antibiofilm activity from Citrobacter freundii. Arch. Microbiol. 2012, 194:575-587.
43. Shanks R.M., Kadouri D.E., Maceachran D.P., O'toole G.A. New yeast recombineering tools for bacteria. Plasmid 2009, 62:88-97.
44. Shen C., Chen Y., Yang C., Chen J., Liu C. Colloid chitin azure is a dispersible, low-cost substrate for chitinase measurements in a sensitive, fast, reproducible assay. J. Biomol. Screen. 2010, 15:213-217.
45. Stella N.A., Kalivoda E.J., O'dee D.M., Nau G.J., Shanks R.M. Catabolite repression control of flagellum production by Serratia marcescens. Res. Microbiol. 2008, 159:562-568.
46. Suh Y., Alpaugh M., Krause K.L., Benedik M.J. Differential secretion of isoforms of Serratia marcescens extracellular nuclease. Appl. Environ. Microbiol. 1995, 61:4083-4088.
47. Tshala-Katumbay D., Monterroso V., Kayton R., Lasarev M., Sabri M., Spencer P. Probing mechanisms of axonopathy. Part I: protein targets of 1,2-diacetylbenzene, the neurotoxic metabolite of aromatic solvent 1,2-diethylbenzene. Toxicol. Sci. 2008, 105:134-141.
48. Wargo M.J., Szwergold B.S., Hogan D.A. Identification of two gene clusters and a transcriptional regulator required for Pseudomonas aeruginosa glycine betaine catabolism. J. Bacteriol. 2008, 190:2690-2699.
49. Watanabe T., Kimura K., Sumiya T., Nikaidou N., Suzuki K., Suzuki M., Taiyoji M., Ferrer S., Regue M. Genetic analysis of the chitinase system of Serratia marcescens 2170. J. Bacteriol. 1997, 179:7111-7117.
50. West S.E., Sample A.K., Runyen-Janecky L.J. The vfr gene product, required for Pseudomonas aeruginosa exotoxin A and protease production, belongs to the cyclic AMP receptor protein family. J. Bacteriol. 1994, 176:7532-7542.