Linked Life Data

1837021

Source:http://linkedlifedata.com/resource/pubmed/id/1837021

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1992-2-7
pubmed:abstractText
The subcellular localization of SecA, a protein essential for the catalysis of general protein export, was studied to better understand its state(s) and function(s) within Escherichia coli cells. In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. Association of SecA protein with the inner membrane required the presence of anionic phospholipids and was modulated by ATP. A fraction of the membrane-bound SecA was found to be integrally associated with the membrane. In the secA51(Ts) mutant 75-95% of SecA protein was found to be membrane associated, independent of the protein export status of the cell, implying that the partitioning of this protein between the cell membrane and cytoplasm may play an important role in its function. secA-lacZ fusions were used to map a membrane association determinant to the amino-terminal quarter of SecA protein sequence. When this portion of SecA protein was expressed within cells, it was found solely in membrane fractions and complemented the growth and protein secretion defect of the secA51(Ts) mutant. This indicates that the membrane is the site of the limiting defect in this mutant and suggests that either SecA functions can be divided into at least two separable activities or that productive interaction between SecA and the amino-terminal fragment can occur in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24420-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1837021-Adenosine Triphosphatases, pubmed-meshheading:1837021-Adenosine Triphosphate, pubmed-meshheading:1837021-Bacterial Proteins, pubmed-meshheading:1837021-Base Sequence, pubmed-meshheading:1837021-Blotting, Western, pubmed-meshheading:1837021-Cardiolipins, pubmed-meshheading:1837021-Cell Fractionation, pubmed-meshheading:1837021-Cell Membrane, pubmed-meshheading:1837021-Chromatography, Gel, pubmed-meshheading:1837021-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1837021-Escherichia coli, pubmed-meshheading:1837021-Escherichia coli Proteins, pubmed-meshheading:1837021-Genes, Bacterial, pubmed-meshheading:1837021-Membrane Transport Proteins, pubmed-meshheading:1837021-Molecular Sequence Data, pubmed-meshheading:1837021-Mutation, pubmed-meshheading:1837021-Phosphatidylglycerols
pubmed:year
1991
pubmed:articleTitle
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.
pubmed:affiliation
Department of Microbiology, State University of New York, Stony Brook 11794.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't