Linked Life Data

8028584

Source:http://linkedlifedata.com/resource/pubmed/id/8028584

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-8-8
pubmed:abstractText
Mutations at the apeA locus in Salmonella typhimurium lead to loss of a soluble enzyme ("protease I") that hydrolyzes the chromogenic endoprotease substrate N-acetyl phenylalanine beta-naphthyl ester. We have isolated pseudorevertants of S. typhimurium apeA mutations that have regained the ability to hydrolyze this compound. These pseudorevertants contain mutations (apeR) that lead to overproduction of a membrane-bound esterase different from protease I. The apeR locus is phage P1 cotransducible with ilvC (83 map units) and is unlinked to apeA. Mutations at still another locus, apeE, lead to loss of the membrane-associated esterase. The apeE locus is P1 cotransducible with purE (12 map units). In an apeE-lacZ operon fusion strain, an apeR mutation increases the level of beta-galactosidase approximately 60-fold. We propose that apeR encodes a repressor of apeE. The evidence available suggests that the ApeE protein is not a protease.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0026-8925
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
243
pubmed:geneSymbol
apeA, apeE, apeR
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
674-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Mutations affecting a regulated, membrane-associated esterase in Salmonella typhimurium LT2.
pubmed:affiliation
Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.