Linked Life Data

8230209

Source:http://linkedlifedata.com/resource/pubmed/id/8230209

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-12-9
pubmed:abstractText
The pyridine nucleotide transhydrogenase of Escherichia coli is an inner membrane protein of two different subunits (alpha and beta). It functions as a proton pump. The highly hydrophilic carboxy-terminal tail of ten amino acid residues in the alpha-subunit determines the correct folding and proper assembly of the beta-subunit leading to a functional enzyme. Premature termination of the alpha-subunit six amino acid residues from the carboxy-terminal end abolishes the activity completely. Although the two subunits are still assembled into the membrane, the conformation of the beta-subunit is perturbed. Systematic truncation and site-directed substitutions revealed that at least one positive charge in the carboxy-terminal region is required for efficient assembly of the two subunits to give a functional enzyme, while a phenylalanine residue, essential for activity, has no apparent effect on the extent of assembly of the two subunits.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-13
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Assembly of multimeric proteins. Effect of mutations in the alpha-subunit on membrane assembly and activity of pyridine nucleotide transhydrogenase.
pubmed:affiliation
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't