Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: Analysis of a possible evolutionary pathway

Stephen Lee, D. K. Ann, E. Wang

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

We previously reported the cloning of a rat S1 cDNA whose deduced amino acid sequence shares high similarity (92%) with that of mammalian elongation factor-1 alpha (EF-1α), a protein involved in the binding of aminoacyl-tRNA to the ribosome during peptide synthesis. We report here the isolation of a full-length cDNA from a mouse brain library and a partial-length cDNA from a human hippocampus library which share extensive sequence similarity to rat S1 cDNA. We show that, as with mammalian EF-1αs, the predicted primary amino acid sequences of rat, mouse, and human S1 are almost identical, except for one conservative substitution. These results indicate that mouse and man contain a second member of the EF-1α gene family, the S1 gene. They also suggest that our result obtained in rat may be extrapolated to mouse and man.

Original languageEnglish (US)
Pages (from-to)1371-1377
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume203
Issue number3
DOIs
StatePublished - 1994
Externally publishedYes

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Peptide Elongation Factor 1
Cloning
Rats
Organism Cloning
Brain
Complementary DNA
Genes
Amino Acid Sequence
Amino Acids
Transfer RNA
Ribosomes
Hippocampus
Substitution reactions
Peptides
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: Analysis of a possible evolutionary pathway",
abstract = "We previously reported the cloning of a rat S1 cDNA whose deduced amino acid sequence shares high similarity (92{\%}) with that of mammalian elongation factor-1 alpha (EF-1α), a protein involved in the binding of aminoacyl-tRNA to the ribosome during peptide synthesis. We report here the isolation of a full-length cDNA from a mouse brain library and a partial-length cDNA from a human hippocampus library which share extensive sequence similarity to rat S1 cDNA. We show that, as with mammalian EF-1αs, the predicted primary amino acid sequences of rat, mouse, and human S1 are almost identical, except for one conservative substitution. These results indicate that mouse and man contain a second member of the EF-1α gene family, the S1 gene. They also suggest that our result obtained in rat may be extrapolated to mouse and man.",
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AU - Wang, E.

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AB - We previously reported the cloning of a rat S1 cDNA whose deduced amino acid sequence shares high similarity (92%) with that of mammalian elongation factor-1 alpha (EF-1α), a protein involved in the binding of aminoacyl-tRNA to the ribosome during peptide synthesis. We report here the isolation of a full-length cDNA from a mouse brain library and a partial-length cDNA from a human hippocampus library which share extensive sequence similarity to rat S1 cDNA. We show that, as with mammalian EF-1αs, the predicted primary amino acid sequences of rat, mouse, and human S1 are almost identical, except for one conservative substitution. These results indicate that mouse and man contain a second member of the EF-1α gene family, the S1 gene. They also suggest that our result obtained in rat may be extrapolated to mouse and man.

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