Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-5-4
pubmed:databankReference
pubmed:abstractText
We have isolated a gene (CAM1) from the yeast Saccharomyces cerevisiae that encodes a protein homologous to the translational cofactor elongation factor-1 gamma (EF-1 gamma) first identified in the brine shrimp Artemia salina. The predicted Cam1 amino acid sequence consists of 415 residues that share 32% identity with the Artemia protein, increasing to 72% when conservative substitutions are included. The calculated M(r) of Cam1p (47,092 Da) is in close agreement with that of EF-1 gamma (M(r) = 49,200 Da), and hydropathy plots of each protein exhibit strikingly similar profiles. Disruption of the CAM1 locus yields four viable meiotic progeny, indicating that under normal growth conditions the Cam1 protein is non-essential. Attempts to elicit a translational phenotype have been unsuccessful. Since EF-1 gamma participates in the regulation of a GTP-binding protein (EF-1 alpha), double mutants with cam1 disruptions and various mutant alleles of known GTP-binding proteins were constructed and examined. No evidence was found for an interaction of CAM1 with TEF1, TEF2, SEC4, YPT1, RAS1, RAS2, CDC6, ARF1, ARF2 or CIN4. The possibility that Cam1p may play a redundant role in the regulation of protein synthesis or another GTP-dependent process is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0749-503X
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
151-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8465602-Amino Acid Sequence, pubmed-meshheading:8465602-Base Sequence, pubmed-meshheading:8465602-Calcium, pubmed-meshheading:8465602-Cell Division, pubmed-meshheading:8465602-Chromosome Mapping, pubmed-meshheading:8465602-Cloning, Molecular, pubmed-meshheading:8465602-Crosses, Genetic, pubmed-meshheading:8465602-DNA Probes, pubmed-meshheading:8465602-Fungal Proteins, pubmed-meshheading:8465602-Genes, Fungal, pubmed-meshheading:8465602-Guanosine Triphosphate, pubmed-meshheading:8465602-Hygromycin B, pubmed-meshheading:8465602-Molecular Sequence Data, pubmed-meshheading:8465602-Mutagenesis, pubmed-meshheading:8465602-Peptide Elongation Factor 1, pubmed-meshheading:8465602-Peptide Elongation Factors, pubmed-meshheading:8465602-Phospholipids, pubmed-meshheading:8465602-Protein Biosynthesis, pubmed-meshheading:8465602-Saccharomyces cerevisiae, pubmed-meshheading:8465602-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8465602-Sequence Analysis, DNA, pubmed-meshheading:8465602-Sequence Homology, Amino Acid
pubmed:year
1993
pubmed:articleTitle
Cloning and genetic characterization of a calcium- and phospholipid-binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor-1 gamma.
pubmed:affiliation
Department of Pharmacology, University of Virginia, Charlottesville 22903.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.