FRAMESHIFT MUTATIONS RESULTING IN CHANGES OF SAME AMINO ACID RESIDUE (140) IN T4 BACTERIOPHAGE LYSOZYME AND IN VIVO CODONS FOR TRP TYR MET VAL AND ILE

被引：19

作者：

TSUGITA, A

INOUYE, M

IMAGAWA, T

NAKANISHI, T

OKADA, Y

EMRICH, J

STREISINGER, G

机构：

[1] Laboratory of Molecular Genetics, Osaka University Medical School Osaka

[2] Institute for Plant Virus Research, Chiba

[3] Institute of Molecular Biology, university of Oregon, Eugene, OR

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1969年 / 41卷 / 03期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0022-2836(69)90281-2

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：

The lysozymes of three new strains of double frameshift mutants of T4 bacteriophage, eJ37eJD3, eJ200eJD4 and eJ25eJD1, were isolated from their respective lysates, and their amino acid sequences were compared with that of the wild-type strain. It was found that Trp138-Tyr-Asn140 in wild-type lysozyme changes to Met-Val-Tyr in eJ37eJD3, Tyr139-Asn140 to Cys-Ile-Ile in eJ200eJD4 and Asn140 to Ile-Ile in eJ25eJD1. From these results, a new hot spot for frameshift mutations has been found at Asn140 and in vivo codons for Trp, Tyr, Met, Val and Ile are thought to be UGG, UAU, AUG and AUA, respectively. Nineteen in vivo codons out of 64 codons have been identified by these results together with our previous results. © 1969.

引用

页码：349 / +

页数：1

共 17 条

[1]

CANFIELD RE, 1963, J BIOL CHEM, V238, P2684

[2] A FRAME-SHIFT MUTATION RESULTING IN DELETION OF 2 BASE PAIRS IN LYSOZYME GENE OF BACTERIOPHAGE T4 [J].