Linked Life Data

7037787

Source:http://linkedlifedata.com/resource/pubmed/id/7037787

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1982-5-27
pubmed:abstractText
A prolonged digestion of colicin E1 with dilute trypsin results in the generation of a trypsin-resistant peptide fragment of the colicin which is approximately one-third of the molecule. The amino acid composition of the fragment, Mr = 20,000, is more nonpolar in nature than the colicin, with the major change in composition being the reduction of the arginine content from 25 residues in the Mr = 56,000 colicin molecule to approximately 1 residue in the fragment. The NH2-terminal amino acid sequence of the tryptic fragment shows no similarity to that of colicin E1. Alignment of this sequence with the complete amino acid sequence of the colicin E1 molecule obtained by others, shows that the fragment occupies all, or almost all, of the COOH-terminal section of the molecule. The fragment behaved similarly to colicin E1, in being able to dissipate a potassium diffusion potential in unilamellar membrane vesicles made of dimyristoylphosphatidylcholine. The fragment was able to dissipate the diffusion potential above and below the temperature region (Tm = 23.5-24 degrees C) of the lipid phase transition in these vesicles, consistent with a channel-like function. The fragment did not show measurable binding to colicin receptor sites on the cell surface, but was much more efficient than colicin E1 in its ability to inhibit proline transport by inner membrane vesicles of Escherichia coli. These data imply that a membrane channel-forming function of the molecule is located in this 20,000 molecular weight region at the COOH-terminal end of the colicin molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3857-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't