Linked Life Data

16169847

Source:http://linkedlifedata.com/resource/pubmed/id/16169847

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2005-11-15
pubmed:abstractText
It has become evident that the process of protein synthesis is performed by many cellular polypeptides acting in concert within the structural confines of protein complexes. In multicellular eukaryotes, one of these assemblies is a multienzyme complex composed of eight proteins that have aminoacyl-tRNA synthetase activities as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. This study uses electron microscopy and three-dimensional reconstruction to explore the arrangement of proteins and tRNA substrates within this "core" multisynthetase complex. Binding of unfractionated tRNA establishes that these molecules are widely distributed on the exterior of the structure. Binding of gold-labeled tRNA(Leu) places leucyl-tRNA synthetase and the bifunctional glutamyl-/prolyl-tRNA synthetase at the base of this asymmetric "V"-shaped particle. A stable cell line has been produced that incorporates hexahistidine-labeled p43 into the multisynthetase complex. Using a gold-labeled nickel-nitrilotriacetic acid probe, the polypeptides of the p43 dimer have been located along one face of the particle. The results of this and previous studies are combined into an initial three-dimensional working model of the multisynthetase complex. This is the first conceptualization of how the protein constituents and tRNA substrates are arrayed within the structural confines of this multiprotein assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
38870-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16169847-Amino Acyl-tRNA Synthetases, pubmed-meshheading:16169847-Aminoacylation, pubmed-meshheading:16169847-Binding Sites, pubmed-meshheading:16169847-Cell Line, pubmed-meshheading:16169847-Cross-Linking Reagents, pubmed-meshheading:16169847-Dimerization, pubmed-meshheading:16169847-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:16169847-Histidine, pubmed-meshheading:16169847-Humans, pubmed-meshheading:16169847-K562 Cells, pubmed-meshheading:16169847-Microscopy, Electron, pubmed-meshheading:16169847-Models, Molecular, pubmed-meshheading:16169847-Multienzyme Complexes, pubmed-meshheading:16169847-Multiprotein Complexes, pubmed-meshheading:16169847-Oligopeptides, pubmed-meshheading:16169847-Peptides, pubmed-meshheading:16169847-Protein Binding, pubmed-meshheading:16169847-Protein Conformation, pubmed-meshheading:16169847-RNA, pubmed-meshheading:16169847-RNA, Transfer
pubmed:year
2005
pubmed:articleTitle
A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins.
pubmed:affiliation
Department of Biology, Tougaloo College, Tougaloo, Mississippi 39174, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.