Linked Life Data

1826108

Source:http://linkedlifedata.com/resource/pubmed/id/1826108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1991-5-1
pubmed:abstractText
SecA interacts with presecretory proteins through recognition of the positive charge at the amino terminus of the signal peptide (Akita, M., Sasaki, S., Matsuyama, S., and Mizushima, S. (1989) J. Biol. Chem. 265, 8164-8169). A large variety of amino-terminal and carboxyl-terminal fragments of SecA were prepared in 6 M guanidine hydrochloride. SecA analogues were then reconstituted from them and examined for their ability to cross-link with [35S]proOmpF-Lpp, a presecretory protein, in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. The reconstituted SecA analogues were active in the cross-linking with proOmpF-Lpp when the SecA fragments used were large enough to structurally complement each other. The cross-linking was signal peptide-dependent and suppressed in the presence of other presecretory proteins. The cross-linking was enhanced in the presence of ATP. The SecA fragments that cross-linked with proOmpF-Lpp were then analyzed on sodium dodecyl sulfate-polyacrylamide gels. The cross-linking preferentially took place on fragments possessing the amino terminus of SecA. Weak cross-linking was also observed with carboxyl-terminal fragments when they were large enough. The smallest amino-terminal and carboxyl-terminal fragments with which the cross-linking was observed were 39 and 72 kDa, respectively. From these results, the region responsible for the cross-linking with presecretory proteins was deduced to be located between amino acid residues 267 and 340 from the amino terminus of SecA. These results are discussed in relation to the structure and function of SecA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/outer membrane protein A precursor...
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6600-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.
pubmed:affiliation
Institute of Applied Microbiology, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't