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大肠杆菌中的核糖体蛋白修饰。II. 缺乏蛋白S18 N端乙酰化的突变体研究。

Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18.

作者信息

Isono K, Isono S

出版信息

Mol Gen Genet. 1980;177(4):645-51. doi: 10.1007/BF00272675.

Abstract

A mutant of Escherichia coli K12 has been isolated which shows an alteration in the ribosomal protein S18. Genetic analyses have revealed that the mutation causing this alteration maps at 99.3 min of the E. coli genetic map, between dnaC and deo. This indicated that the mutation has occurred in a gene different from the structural gene for this protein which has been located at 94 min. From the N-terminal amino acid sequence analysis it is concluded that the mutation has resulted in loss of the N-terminal acetyl group of this protein. The gene which is affected in this mutant is termed rimI that most likely specifies an enzyme acetylating the N-terminal alanine of protein S18. The mutation does not affect the acetylation of two other ribosomal proteins, S5 and L12, both of which are known to be acetylated in wild-type E. coli K12.

摘要

已分离出大肠杆菌K12的一个突变体,其核糖体蛋白S18发生了改变。遗传分析表明,导致这种改变的突变位于大肠杆菌遗传图谱的99.3分钟处,在dnaC和deo之间。这表明该突变发生在一个与该蛋白质结构基因不同的基因中,该结构基因位于94分钟处。从N端氨基酸序列分析得出结论,该突变导致该蛋白质的N端乙酰基缺失。在这个突变体中受影响的基因被称为rimI,它很可能指定一种使蛋白质S18的N端丙氨酸乙酰化的酶。该突变不影响另外两种核糖体蛋白S5和L12的乙酰化,已知这两种蛋白在野生型大肠杆菌K12中会被乙酰化。

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