Linked Life Data

2569467

Source:http://linkedlifedata.com/resource/pubmed/id/2569467

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1989-9-13
pubmed:abstractText
Elongation Factor 1 alpha (EF-1 alpha), an important eukaryotic translation factor, transports charged aminoacyl-tRNA from the cytosol to the ribosomes during poly-peptide synthesis. Metabolic radiolabeling with [3H] ethanolamine shows that, in all cells examined, EF-1 alpha is the major radiolabeled protein. Radiolabeled EF-1 alpha has an apparent Mr = 53,000 and a basic isoelectric point. It is cytosolic and does not contain N-linked oligosaccharides. Trypsin digestion of murine EF-1 alpha generated two major [3H]ethanolamine-labeled peptides. Three peptides were sequenced and were identical to two distinct regions of the human EF-1 alpha protein. Blank sequencing cycles coinciding with glutamic acid in the human cDNA-derived sequence were also found to release [3H]ethanolamine, and compositional analysis of these peptides confirmed the presence of glutamic acid. Dansylation analysis demonstrates that the amine group of the ethanolamine is blocked. These results indicate that EF-1 alpha is posttranslationally modified by the covalent attachment of ethanolamine via an amide bond to at least two specific glutamic acid residues (Glu-301 and Glu-374). The hydroxyl group of the attached ethanolamine was shown by mass spectrometry and compositional analysis, to be further modified by the addition of a phosphoglycerol unit. This novel posttranslational modification may represent an important alteration of EF-1 alpha, comparable to the regulatory effects of posttranslational methylation of EF-1 alpha lysine residues.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14334-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2569467-Amino Acid Sequence, pubmed-meshheading:2569467-Animals, pubmed-meshheading:2569467-Cell Line, pubmed-meshheading:2569467-Cricetinae, pubmed-meshheading:2569467-Cricetulus, pubmed-meshheading:2569467-Ethanolamine, pubmed-meshheading:2569467-Ethanolamines, pubmed-meshheading:2569467-Glutamates, pubmed-meshheading:2569467-Glutamic Acid, pubmed-meshheading:2569467-Glycerophosphates, pubmed-meshheading:2569467-Humans, pubmed-meshheading:2569467-Mass Spectrometry, pubmed-meshheading:2569467-Mice, pubmed-meshheading:2569467-Molecular Sequence Data, pubmed-meshheading:2569467-Molecular Weight, pubmed-meshheading:2569467-Peptide Elongation Factor 1, pubmed-meshheading:2569467-Peptide Elongation Factors, pubmed-meshheading:2569467-Peptide Fragments, pubmed-meshheading:2569467-Protein Processing, Post-Translational, pubmed-meshheading:2569467-Thymoma, pubmed-meshheading:2569467-Tritium
pubmed:year
1989
pubmed:articleTitle
Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.