TY - JOUR
T1 - Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5)
AU - Si, Kausik
AU - Das, Kallol
AU - Maitra, Umadas
PY - 1996
Y1 - 1996
N2 - Eukaryotic translation initiation factor 5 (eIF-5) interacts with the 40 S initiation complex (40S · mRNA · Met-tRNA(f) · eIF-2 · GTP) to promote the hydrolysis of bound GTP with the concomitant joining of the 60 S ribosomal subunit to the 40 S initiation complex to form a functional 80 S initiation complex. In this paper, the multiple mRNAs that encode mammalian eIF-5 have been characterized. In rat tissues, three major eIF-5 mRNAs of 3.5, 2.8, and 2.2 kilobases in length are detected. All major eIF-5 mRNAs are initiated from a single transcription initiation site, contain identical 5'- untranslated and coding regions, but differ from one another only in the length of their 3'-untranslated regions. The different lengths of the 3'- untranslated region of eIF-5 mRNAs are generated by the use of alternative polyadenylation signals. Additionally, we demonstrate tissue-specific variations in eIF-5 mRNA expression as well as preference for polyadenylation sites. These results should lead to increased understanding of the regulation of eIF-5 gene expression.
AB - Eukaryotic translation initiation factor 5 (eIF-5) interacts with the 40 S initiation complex (40S · mRNA · Met-tRNA(f) · eIF-2 · GTP) to promote the hydrolysis of bound GTP with the concomitant joining of the 60 S ribosomal subunit to the 40 S initiation complex to form a functional 80 S initiation complex. In this paper, the multiple mRNAs that encode mammalian eIF-5 have been characterized. In rat tissues, three major eIF-5 mRNAs of 3.5, 2.8, and 2.2 kilobases in length are detected. All major eIF-5 mRNAs are initiated from a single transcription initiation site, contain identical 5'- untranslated and coding regions, but differ from one another only in the length of their 3'-untranslated regions. The different lengths of the 3'- untranslated region of eIF-5 mRNAs are generated by the use of alternative polyadenylation signals. Additionally, we demonstrate tissue-specific variations in eIF-5 mRNA expression as well as preference for polyadenylation sites. These results should lead to increased understanding of the regulation of eIF-5 gene expression.
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U2 - 10.1074/jbc.271.28.16934
DO - 10.1074/jbc.271.28.16934
M3 - Article
C2 - 8663286
AN - SCOPUS:0029938853
SN - 0021-9258
VL - 271
SP - 16934
EP - 16938
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 28
ER -