Linked Life Data

15919996

Source:http://linkedlifedata.com/resource/pubmed/id/15919996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5726
pubmed:dateCreated
2005-5-27
pubmed:abstractText
The protein complement of cellular membranes is notoriously resistant to standard proteomic analysis and structural studies. As a result, membrane proteomes remain ill-defined. Here, we report a global topology analysis of the Escherichia coli inner membrane proteome. Using C-terminal tagging with the alkaline phosphatase and green fluorescent protein, we established the periplasmic or cytoplasmic locations of the C termini for 601 inner membrane proteins. By constraining a topology prediction algorithm with this data, we derived high-quality topology models for the 601 proteins, providing a firm foundation for future functional studies of this and other membrane proteomes. We also estimated the overexpression potential for 397 green fluorescent protein fusions; the results suggest that a large fraction of all inner membrane proteins can be produced in sufficient quantities for biochemical and structural work.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
308
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1321-3
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Global topology analysis of the Escherichia coli inner membrane proteome.
pubmed:affiliation
Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't