Linked Life Data

8521840

Source:http://linkedlifedata.com/resource/pubmed/id/8521840

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-1-23
pubmed:abstractText
In eukaryotes, the cotranslational targeting of proteins to the endoplasmic reticular membrane is initially mediated by the signal-recognition particle (SRP), a ribonucleoprotein complex consisting of the 7SL RNA and six protein subunits. Since the discovery of sequence homology between (a) the Escherichia coli 4.5S RNA (Ffs) and 7SL RNA, and (b) the E. coli P48 (Ffh) and SRP 54-kDa subunit, more evidence has been obtained that E. coli also possesses an SRP-type pathway that acts in the translocation of secreted proteins. Such a pathway could possibly be involved in the cotranslational integration of hydrophobic membrane proteins that cannot be effectively targeted post-translationally due to folding and aggregation. In this study, we report that disruption of the E. coli SRP complex with a dominant lethal 4.5S RNA mutant in vivo prevents functional membrane integration of the E. coli lactose permease (LacY). Likewise, depletion of the P48 (Ffh) protein also results in a decrease in the amount of functional LacY inserted into the E. coli plasma membrane. In direct contrast, inhibition of SecA function does not affect LacY integration. These results suggest a major function of the bacterial SRP in the targeting and subsequent integration of hydrophobic membrane proteins as opposed to SecA mediating the post-translational targeting of secretory proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
233
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
766-71
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle.
pubmed:affiliation
Institut für Physikalische Biochemie, Universität München, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't