Linked Life Data

2559435

Source:http://linkedlifedata.com/resource/pubmed/id/2559435

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-3-5
pubmed:abstractText
The roles of submolecular regions of OmpF and OmpC, major outer membrane proteins of Escherichia coli, as concerns their biogenesis, structure and function were studied using a large number of chimeric genes constructed from the ompF and ompC genes through single or double homologous in vivo recombination. When recombination between the two genes took place at certain regions of their central regions, no chimeric protein was detected, irrespective of whether the amino-terminal and carboxy-terminal regions were derived from OmpF or OmpC. Biochemical studies revealed that these proteins were synthesized and exported across the cytoplasmic membrane normally, but that they were not properly assembled into the outer membrane and hence were degraded rapidly. Characterization of these chimeric proteins, in which recombination between OmpF and OmpC took place once or twice, suggested that the central region of each of these proteins plays an important role in the respective assembly, whereas the roles of the amino-terminal and carboxy-terminal regions may be marginal. Functional characterization of these chimeric proteins revealed the regions important for the receptor functions of OmpF and OmpC for phages TuIa and TuIb, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0923-2508
pubmed:author
pubmed:issnType
Print
pubmed:volume
140
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Structural and functional characterization of the OmpF and OmpC porins of the Escherichia coli outer membrane: studies involving chimeric proteins.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't