Plasmid regulation and temperature-sensitive behavior of the Yersinia pestis penicillin-binding proteins.
Six major bands corresponding to penicillin-binding proteins (PBPs) with molecular weights ranging from 43,000 to 97,000 were detected in cell envelopes of Yersinia pestis EV76 grown at 28 degrees C. When cells were transferred to 37 degrees C and incubated for extended periods of time, the amounts of all PBPs, except for PBP2, were gradually reduced in cell envelopes of a strain carrying a 75-kb virulence-associated plasmid (as measured by penicillin-binding capacity), whereas in a strain cured of the plasmid, all PBPs were stable. The results indicated that the stability and/or the expression of Y. pestis PBPs is affected by a temperature-inducible pathway associated with the virulence-associated plasmid.
Ferreira
R C
RC
Instituto de Biofísica Carlos Chagas Filho-CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Brazil.
Park
J T
JT
Ferreira
L C
LC
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000032:analysis*; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000032:analysis*; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D010957:Plasmids; D013696:Temperature; D015010:Yersinia pestis / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase