BACTERIOPHAGE-T4 RIIB-PROTEIN SYNTHESIS WITH A TEMPERATURE-SENSITIVE MUTATION IN THE RIIB-INITIATION CODON

被引:10
作者
BELIN, D
机构
[1] Département de Biologie Moléculaire, Université de Genève, Genève 4, CH-1211, 30, Quai Ernest-Ansermet
来源
MOLECULAR & GENERAL GENETICS | 1979年 / 171卷 / 01期
关键词
D O I
10.1007/BF00274012
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In protein synthesis, the incorporation of an N-terminal formylmethionine residue is directed by an initiation codon. The most frequently used codon is AUG, although initiation at GUG and UUG codons has also been observed. The HD263 mutation is an AUG to AUA change in the rIIB initiation codon. Evidence is presented here that wild type and HD263 rIIB proteins, whether synthesized in vivo or in vitro, have identical fmet peptides. It is concluded that translation began at the AUA mutant initiation codon in vitro and in phage T4 infected cells. In the in vitro translation system used in these studies, the rIIB protein synthesized at 25° no longer contains the N-terminal formyl group whereas a large proportion of the formyl group is retained at 37°. © 1979 Springer-Verlag.
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页码:35 / 42
页数:8
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