Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae

Cloning, characterization, and expression of the gene encoding the 45,346-Da protein

Debabrata Chakravarti, Umadas Maitra

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Eukaryotic translation initiation factor 5 (eIF-5) catalyzes hydrolysis of GTP bound to a 40 S ribosomal initiation complex with the subsequent joining of a 60 S ribosomal subunit to form an 80 S initiation complex. The yeast gene that encodes eIF-5, designated TIF5, has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. TIF5 is a single-copy gene that maps on yeast chromosome XVI and is essential for cell viability. The gene contains an intron-free open reading frame that encodes a protein of calculated Mr 45,346 in close agreement with the apparent molecular weight of eIF-5 isolated from yeast cells. Sequence analysis of the gene reveals several interesting features. First, the presence of two inframe translational start sites located 51 base pairs apart suggests the possibility that two proteins, differing by an amino-terminal extension of 17 amino acids, could be generated from the TIF5 gene via differential translational starts. This would explain the presence, in yeast cell lysates, of two forms of eIF-5 differing in molecular weight by about 2,000. Second, the predicted amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.

Original languageEnglish (US)
Pages (from-to)10524-10533
Number of pages10
JournalJournal of Biological Chemistry
Volume268
Issue number14
StatePublished - May 15 1993

Fingerprint

Eukaryotic Initiation Factor-5
Eukaryotic Initiation Factors
Gene encoding
Cloning
Yeast
Saccharomyces cerevisiae
Organism Cloning
Gene Expression
Genes
Yeasts
Proteins
Cells
Molecular Weight
Molecular weight
Amino Acids
Ribosome Subunits
Amino Acid Motifs
GTP Phosphohydrolases
Chromosomes
Guanosine Triphosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae : Cloning, characterization, and expression of the gene encoding the 45,346-Da protein. / Chakravarti, Debabrata; Maitra, Umadas.

In: Journal of Biological Chemistry, Vol. 268, No. 14, 15.05.1993, p. 10524-10533.

Research output: Contribution to journalArticle

@article{4133b1cba4864d11a63b03458ed49dd9,
title = "Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae: Cloning, characterization, and expression of the gene encoding the 45,346-Da protein",
abstract = "Eukaryotic translation initiation factor 5 (eIF-5) catalyzes hydrolysis of GTP bound to a 40 S ribosomal initiation complex with the subsequent joining of a 60 S ribosomal subunit to form an 80 S initiation complex. The yeast gene that encodes eIF-5, designated TIF5, has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. TIF5 is a single-copy gene that maps on yeast chromosome XVI and is essential for cell viability. The gene contains an intron-free open reading frame that encodes a protein of calculated Mr 45,346 in close agreement with the apparent molecular weight of eIF-5 isolated from yeast cells. Sequence analysis of the gene reveals several interesting features. First, the presence of two inframe translational start sites located 51 base pairs apart suggests the possibility that two proteins, differing by an amino-terminal extension of 17 amino acids, could be generated from the TIF5 gene via differential translational starts. This would explain the presence, in yeast cell lysates, of two forms of eIF-5 differing in molecular weight by about 2,000. Second, the predicted amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.",
author = "Debabrata Chakravarti and Umadas Maitra",
year = "1993",
month = "5",
day = "15",
language = "English (US)",
volume = "268",
pages = "10524--10533",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae

T2 - Cloning, characterization, and expression of the gene encoding the 45,346-Da protein

AU - Chakravarti, Debabrata

AU - Maitra, Umadas

PY - 1993/5/15

Y1 - 1993/5/15

N2 - Eukaryotic translation initiation factor 5 (eIF-5) catalyzes hydrolysis of GTP bound to a 40 S ribosomal initiation complex with the subsequent joining of a 60 S ribosomal subunit to form an 80 S initiation complex. The yeast gene that encodes eIF-5, designated TIF5, has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. TIF5 is a single-copy gene that maps on yeast chromosome XVI and is essential for cell viability. The gene contains an intron-free open reading frame that encodes a protein of calculated Mr 45,346 in close agreement with the apparent molecular weight of eIF-5 isolated from yeast cells. Sequence analysis of the gene reveals several interesting features. First, the presence of two inframe translational start sites located 51 base pairs apart suggests the possibility that two proteins, differing by an amino-terminal extension of 17 amino acids, could be generated from the TIF5 gene via differential translational starts. This would explain the presence, in yeast cell lysates, of two forms of eIF-5 differing in molecular weight by about 2,000. Second, the predicted amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.

AB - Eukaryotic translation initiation factor 5 (eIF-5) catalyzes hydrolysis of GTP bound to a 40 S ribosomal initiation complex with the subsequent joining of a 60 S ribosomal subunit to form an 80 S initiation complex. The yeast gene that encodes eIF-5, designated TIF5, has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. TIF5 is a single-copy gene that maps on yeast chromosome XVI and is essential for cell viability. The gene contains an intron-free open reading frame that encodes a protein of calculated Mr 45,346 in close agreement with the apparent molecular weight of eIF-5 isolated from yeast cells. Sequence analysis of the gene reveals several interesting features. First, the presence of two inframe translational start sites located 51 base pairs apart suggests the possibility that two proteins, differing by an amino-terminal extension of 17 amino acids, could be generated from the TIF5 gene via differential translational starts. This would explain the presence, in yeast cell lysates, of two forms of eIF-5 differing in molecular weight by about 2,000. Second, the predicted amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.

UR - http://www.scopus.com/inward/record.url?scp=0027318447&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027318447&partnerID=8YFLogxK

M3 - Article

VL - 268

SP - 10524

EP - 10533

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -