Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases

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dc.contributor.author Telkov, M. V.
dc.contributor.author Demina, G. R.
dc.contributor.author Voloshin, S. A.
dc.contributor.author Salina, Elena G.
dc.contributor.author Dudik, T. V.
dc.contributor.author Stekhanova, T. N.
dc.contributor.author Mukamolova, Galina V.
dc.contributor.author Kazaryan, K. A.
dc.contributor.author Goncharenko, A. V.
dc.contributor.author Young, Michael
dc.contributor.author Kaprelyants, Arseny S.
dc.date.accessioned 2009-07-21T15:15:33Z
dc.date.available 2009-07-21T15:15:33Z
dc.date.issued 2006-04-01
dc.identifier.citation Telkov , M V , Demina , G R , Voloshin , S A , Salina , E G , Dudik , T V , Stekhanova , T N , Mukamolova , G V , Kazaryan , K A , Goncharenko , A V , Young , M & Kaprelyants , A S 2006 , ' Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases ' Biochemistry (Moscow) , vol 71 , no. 4 , pp. 414-422 . en
dc.identifier.issn 0006-2979
dc.identifier.other PURE: 113055
dc.identifier.other dspace: 2160/2701
dc.identifier.uri http://hdl.handle.net/2160/2701
dc.identifier.uri http://www.ncbi.nlm.nih.gov/pubmed/16615861 en
dc.description Telkov, M. V., Demina, G. R., Voloshin, S. A., Salina, E. G., Dudik, T. V., Stekhanova, T. N., Mukamolova, G. V., Kazaryan, K. A., Goncharenko, A. V., Young, M., Kaprelyants, A. S. (2006). Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases. Biochemistry-Moscow, 71 (4), 414-422. en
dc.description.abstract The secreted Micrococcus luteus protein, Rpf, is required for successful resuscitation of dormant 'non-culturable' M. luteus cells and for growth stimulation in poor media. The biochemical mechanism of Rpf action remained unknown. Theoretical predictions of Rpf domain architecture and organization, together with a recent NMR analysis of the protein structure, indicate that the conserved Rpf domain has a lysozyme-like fold. In the present study, we found that both the secreted native protein and the recombinant protein lyse crude preparations of M. luteus cell walls. They also hydrolyze 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside, a synthetic substrate for peptidoglycan muramidases, with optimum activity at pH 6. The Rpf protein also has weak proteolytic activity against N-CBZ-Gly-Gly-Arg-beta-naphthylamide, a substrate for trypsin-like enzymes. Rpf activity towards 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside was reduced when the glutamate residue at position 54, invariant for all Rpf family proteins and presumably involved in catalysis, was altered. The same amino acid substitution resulted in impaired resuscitation activity of Rpf. The data indicate that Rpf is a peptidoglycan-hydrolyzing enzyme, and strongly suggest that this specific activity is responsible for its growth promotion and resuscitation activity. A possible mechanism of Rpf-mediated resuscitation is discussed. en
dc.format.extent 9 en
dc.language.iso eng
dc.relation.ispartof Biochemistry (Moscow) en
dc.subject proteins of the Rpf family en
dc.subject pepriodoglycan hydrolases en
dc.subject "non-culturable" cells en
dc.title Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1134/S0006297906040092
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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