Linked Life Data

17163776

Source:http://linkedlifedata.com/resource/pubmed/id/17163776

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2006-12-13
pubmed:abstractText
A key function of biological membranes is to exclude toxic small molecules while allowing influx of nutrients. Cells achieve this by controlling the composition of different types of proteins and lipids within the membrane by a process called membrane biogenesis. We have recently proposed a strategy to identify genes involved in membrane biogenesis in Gram-negative bacteria such as Escherichia coli by selecting for suppressors of mutations that render the outer membrane (OM) leaky. We predicted that different small molecules could select different suppressors because mutations that answer a specific selection will correct the membrane permeability defect to different degrees depending on the structure of the small molecule. We have tested this hypothesis by selecting for resistance to bile acids in an imp4213 strain, which contains a compromised OM owing to a defect in lipopolysaccharide biogenesis. We report here that a suppressor mutation in yaeT , which specifies an essential protein involved in the assembly of beta-barrel proteins in the OM, confers resistance to a specific subset of bile acids in the imp4213 strain. YaeT is conserved from bacteria to man because it is involved in OM biogenesis in mitochondria and chloroplasts. These results demonstrate that structurally different toxic small molecules select different, and highly specific, genetic solutions for correcting membrane-permeability defects. The remarkable chemical specificity of the imp4213 suppressors provides insights into the molecular nature of the OM permeability barrier.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1554-8937
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
385-95
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Probing the barrier function of the outer membrane with chemical conditionality.
pubmed:affiliation
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural