Show simple item record Telkov, M. V. Demina, G. R. Voloshin, S. A. Salina, Elena G. Dudik, T. V. Stekhanova, T. N. Mukamolova, Galina V. Kazaryan, K. A. Goncharenko, A. V. Young, Michael Kaprelyants, Arseny S. 2009-07-21T15:15:33Z 2009-07-21T15:15:33Z 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 ' Биохимия , vol 71 , no. 4 , pp. 414-422 . , 10.1134/S0006297906040092 en
dc.identifier.issn 0006-2979
dc.identifier.other PURE: 113055
dc.identifier.other dspace: 2160/2701
dc.identifier.uri 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 Биохимия 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 /dk/atira/pure/researchoutput/researchoutputtypes/contributiontojournal/article en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en

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