Linked Life Data

1931946

Source:http://linkedlifedata.com/resource/pubmed/id/1931946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
1991-11-25
pubmed:abstractText
Peptides corresponding to the wild-type signal sequence of the Escherichia coli outer membrane protein OmpA and several mutants have been synthesized and characterized biophysically. The mutations were designed collaboratively with Inouye and co-workers to test the understanding of the critical characteristics of signal sequences required for their functions. The in vivo results for these mutants have been reported [Lehnhardt, S., Pollitt, S., & Inouye, M. (1987) J. Biol. Chem. 262, 1716-1719; Goldstein, J., Lehnhardt, S., & Inouye, M. (1990) J. Bacteriol. 172, 1225-1231; Goldstein, J., Lehnhardt, S., & Inouye, M. (1991) J. Biol. Chem. 266, 14413-14417], and the present paper compares the conformational and membrane-interactive properties of six of the OmpA signal peptides. Peptides corresponding to functional OmpA signal sequences in vivo are predominantly alpha-helical in membrane-mimetic environments and insert readily into phospholipid bilayers. Nonfunctional OmpA signal peptides may have high helical content but do not penetrate deeply into the acyl chain region of bilayers. The ability of the signal peptides to insert into membranes and their in vivo function correlate with the residue-average hydrophobicity of their hydrophobic cores. The results obtained on OmpA signal peptides parallel closely our previous observations on peptides corresponding to the LamB signal sequence and mutants, arguing that the critical biophysical properties of signal sequences are general despite their lack of primary sequence identity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10155-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function.
pubmed:affiliation
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9041.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't