Regulation of Yersinia enterocolitica mal genes by malT and Mlc proteins

• Autorzy: Raczkowska A , Brzostkowska M. , Brzostek K.
• Języki publikacji: EN

Abstrakty

EN

To show the role of MalT protein in the regulation of mal genes, encoding proteins involved in transport and metabolism of maltose/ maltodextrins in Yersinia enterocolitica, we constructed a malT mutant which was characterized by a strong reduction in maltose transport and a loss of MBP protein. We also studied the influence of MalT activity on the production of Yop proteins in Y. enterocolitica and found that the level of these virulence factors is not changed in the malT mutant. Subsequently, transcriptional fusion malT::lacZYA was applied to study the activity of malT promoter. Monitoring of β-galactosidase activity suggests the influence of catabolic repression on malT transcription, since the activity of ma/Tpromoter was decreased twofold in the presence of glucose. Furthermore, Mlc protein was identified in Y. enterocolitica as a factor regulating the transcription of malT. We observed a two-fold increase in the level of malT transcription in the mlc mutant background. Moreover, overproduction of Mlc protein strongly inhibited the activity of malT promoter. Thus, the data presented in this study suggest that the level of mal gene expression in Y enterocolitica may be regulated by two proteins: MalT, the activator of mal transcription and Mlc, the repressor of malT expression.

Słowa kluczowe

EN

gene expression; MBP protein loss; Yersinia enterocolitica; MalT protein; maltose transport; mal gene; maltose; beta-galactosidase; Mlc protein; gene; Yop protein; maltodextrin; gene regulation; malT mutant

• Wydawca: -
• Czasopismo: Polish Journal of Microbiology
• Rocznik: 2008
• Tom: 57
• Numer: 1
• Opis fizyczny: p.19-26,fig.,ref.

Twórcy

autor

Raczkowska A

• University of Warsaw, Miecznikowa 1, 02-089 Warsaw, Poland

autor

Brzostkowska M.

autor

Brzostek K.

Bibliografia

• Bäumler A.R., M. Tsolis, A.W.M. Van Der Velden, I.S. Stojiljkovic and F. Anic Heffron. 1996. Identification of a new iron regulated locus of Salmonella typhi. Gene 183: 207-213.
• Bohm A. and W. Boos. 2004. Gene regulation in prokaryotes by subcellular relocalization of transcription factors. Curr. Microbiol. 1: 151-156.
• Boos W. and H. Schuman. 1998. Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62: 204-229.
• Brzostek K. and A. Raczkowska. 2001. The level of Yop proteins secreted by Yersinia enterocolitica is changed in maltose mutants. FEMS Microbiol. Lett. 204: 95-100.
• Brzostek K., H. Heleszko and J. Hrebenda. 1993. Maltoporins and maltose-binding proteins of Yersinia enterocolitica. J. Gen. Microbiol. 139: 195-201.
• Brzostek K., H. Heleszko and J. Hrebenda. 1995. Production of Escherichia coli LamB protein in Yersinia enterocolitica. FEMS Microbiol. Lett. 127: 17-21.
• Chapon C. 1982. Role of the catabolite activator protein in the maltose regulon of Escherichia coli. J. Bacteriol. 150: 722-729.
• Cornells G.R., A. Boland, A.P. Boyd, C. Geuijen, M. Iriarte, C. Neyt, M.P. Sory and I. Stainier. 1998. The virulence plasmid of Yersinia, an antihost genome. Microbiol. Mol. Biol. Rev. 62: 1315-1352.
• Decker K., J. Plumbridge and W. Boss. 1998. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol. Micobiol. 27: 281-390.
• Ehrmann M. and W. Boos. 1987. Identification of endogenous inducers of the mal system in Escherichia coli. J. Bacteriol. 169: 3539-3545.
• Figurski D.H. and D.R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76: 1648-1652.
• Joly N., A. Böhm, W. Boos and E. Richet. 2004. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding. J. Biol. Chem. 279: 33123-33130.
• Joly N., O. Danot, A. Schlegel, W. Boos and E. Richet. 2002. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J. Biol. Chem. 277: 16606-16613.
• Kim S.Y., T.W. Nam, D. Shin, B.M. Koo. and Y.J. Seok. 1999. Purification of Mlc and analysis of its effect on the pts expression in Escherichia coli. J. Biol. Chem. 274: 25398-25402.
• Kinder S.A., J.L. Badger, G.O. Bryant, J.C. Pepe and V.G. Miller. 1993. Cloning of the Yeril restriction endonuclease and methylase from Yersinia enterocolitica serotype 08 and construction of a transformable R⁻M⁺ mutant. Gene 136: 271-275.
• Konishi Y., A. Amemura, S. Tanabe and T. Harada. 1979. Immunological study of pullulanase from Klebsiella strains and the occurrence of this enzyme in the Enterobacteriaceae. Int. J. Syst. Bacteriol. 29: 13-18.
• Kovach M.E., P.H. Elzer, D.S. Hill, G.T. Robertson, M.A. Farris, R.M. Roop II and K.M. Peterson. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166: 175-176.
• Lang H., G. Jonson, J. Holmgren and E.T. Palva. 1994. The maltose regulon of Vibrio cholerae affects production and secretion of virulence factors. Infect. Immun. 62: 4781-4788.
• Miller J.H. 1972. Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
• Navarro L., N.M. Alto and J.E. Dixon. 2005. Functions of the Yersinia effector proteins in inhibiting host immune responses. Curr. Opin. Microbiol. 8: 21-27.
• Plumbridge J. 1998. Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol. Microbiol. 27: 369-379.
• Plumbridge J. 1999. Expression of the phosphotransferase system both mediates and is mediated by Mlc regulation in Escherichia coli. Mol. Microbiol. 33: 260-273.
• Raibaud O. and E. Richet. 1987. Maltotriose is the inducer of the maltose regulon. J. Bacteriol. 169: 3059-3061.
• Richet E. and O. Raibaud. 1987. Purification and properties of the MalT protein, the transcription activator of the Escherichia coli maltose regulon. J. Biol. Chem. 262: 12647-12653.
• Sambrook J., E.F. Fritsch and T. Maniatis. 1989. Molecular Cloning: a Laboratory Manual, 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
• Schlegel A., O. Danot, E. Richet, T. Ferenci and W. Boos. 2002. The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J. Bacteriol. 184: 3069-3077.
• Schneider E., S. Freundlieb, S. Tapio and W. Boos. 1992. Molecular characterization of the MalT-dependent periplasinic α-amylase of Escherichia coli encoded by malS. J. Biol. Chem. 267: 5148-5154.
• Schreiber V., C. Steegborn, T. Clausen, W. Boos and E. Richet. 2000. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol. Microbiol. 35: 765-776.
• Seitz S., S.J. Lee, C. Pennetier, W. Boos and J. Plumbridge. 2003. Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose-specific phosphotransferase system in Escherichia coli. J. Biol. Chem. 278: 10744-10751.
• Simon R., U. Priefer and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Biotechnology 1: 784-791.
• Tanaka Y., H. Kimata and H. Aiba. 2000. A novel regulatory role of glucose transporter of Escherichia coli: membrane sequestration of a global repressor Mlc. EMBO J. 19: 5344-5352.