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dc.contributor.authorSodeinde, Olanrewaju A.
dc.contributor.authorSample, Allen K.
dc.contributor.authorBrubaker, Robert R.
dc.contributor.authorGoguen, Jon D.
dc.date2022-08-11T08:08:48.000
dc.date.accessioned2022-08-23T16:08:56Z
dc.date.available2022-08-23T16:08:56Z
dc.date.issued1988-10-01
dc.date.submitted2009-01-12
dc.identifier.citation<p>Infect Immun. 1988 Oct;56(10):2749-52.</p>
dc.identifier.issn0019-9567 (Print)
dc.identifier.pmid2843471
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32573
dc.description.abstractThe related family of virulence plasmids found in the three major pathogens of the genus Yersinia all have the ability to encode a set of outer membrane proteins. In Y. enterocolitica and Y. pseudotuberculosis, these proteins are major constituents of the outer membrane when their synthesis is fully induced. In contrast, they have been difficult to detect in Y. pestis. It has recently been established that Y. pestis does synthesize these proteins, but that they are rapidly degraded due to some activity determined by the 9.5-kilobase plasmid commonly found in Y. pestis strains. We show that mutations in the pla gene of this plasmid, which encodes both the plasminogen activator and coagulase activities, blocked this degradation. A cloned 1.4-kilobase DNA fragment carrying pla was also sufficient to cause degradation in the absence of the 9.5-kilobase plasmid.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=2843471&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC259639/
dc.subjectBacterial Outer Membrane Proteins; Coagulase; DNA Mutational Analysis; DNA Transposable Elements; Genes, Bacterial; Immunosorbent Techniques; Molecular Weight; Plasmids; Plasminogen Activators; Yersinia pestis
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titlePlasminogen activator/coagulase gene of Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins
dc.typeJournal Article
dc.source.journaltitleInfection and immunity
dc.source.volume56
dc.source.issue10
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1136
dc.identifier.contextkey692129
html.description.abstract<p>The related family of virulence plasmids found in the three major pathogens of the genus Yersinia all have the ability to encode a set of outer membrane proteins. In Y. enterocolitica and Y. pseudotuberculosis, these proteins are major constituents of the outer membrane when their synthesis is fully induced. In contrast, they have been difficult to detect in Y. pestis. It has recently been established that Y. pestis does synthesize these proteins, but that they are rapidly degraded due to some activity determined by the 9.5-kilobase plasmid commonly found in Y. pestis strains. We show that mutations in the pla gene of this plasmid, which encodes both the plasminogen activator and coagulase activities, blocked this degradation. A cloned 1.4-kilobase DNA fragment carrying pla was also sufficient to cause degradation in the absence of the 9.5-kilobase plasmid.</p>
dc.identifier.submissionpathgsbs_sp/1136
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages2749-52


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