Abstract
Eukaryotic translation initiation factor 5 (eIF-5) catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S·AUG·Met-tRNAf-eIF-2·GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the formation of a functional 80S initiation complex. A rat cDNA that encodes eIF-5 has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. The 3.55-kb cDNA encodes a protein of 429 amino acids (calculated Mr 48,926) with properties that are similar to eIF-5 isolated from rabbit reticulocyte lysates. The deduced amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.
Original language | English (US) |
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Pages (from-to) | 3058-3062 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 90 |
Issue number | 7 |
DOIs | |
State | Published - Apr 1 1993 |
Externally published | Yes |
Keywords
- GTP hydrolysis
- GTPase superfamily proteins
- Protein synthesis
ASJC Scopus subject areas
- General