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枯草芽孢杆菌细胞内丝氨酸蛋白酶突变体的构建与特性

Construction and properties of an intracellular serine protease mutant of Bacillus subtilis.

作者信息

Band L, Henner D J, Ruppen M

出版信息

J Bacteriol. 1987 Jan;169(1):444-6. doi: 10.1128/jb.169.1.444-446.1987.

DOI:10.1128/jb.169.1.444-446.1987
PMID:3098735
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC211792/
Abstract

An intracellular serine protease (ISP-1) mutant of Bacillus subtilis was created by introducing a frameshift into the coding region of the cloned gene. Intracellular protease activity in the mutant was very low, yet sporulation in both nutrient broth and minimal medium was normal. The rate of bulk protein turnover in the mutant was slightly slower than that in the wild-type strain. These results suggest that the gene for ISP-1 is not essential and that ISP-1 is not the major enzyme involved in protein turnover during sporulation.

摘要

通过在克隆基因的编码区引入移码突变，构建了枯草芽孢杆菌的一种细胞内丝氨酸蛋白酶（ISP-1）突变体。该突变体中的细胞内蛋白酶活性非常低，但在营养肉汤和基本培养基中的孢子形成均正常。突变体中总蛋白质周转速率略慢于野生型菌株。这些结果表明，ISP-1基因并非必需，且ISP-1不是孢子形成过程中参与蛋白质周转的主要酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/084b/211792/958dc18dc079/jbacter00191-0463-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/084b/211792/958dc18dc079/jbacter00191-0463-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/084b/211792/958dc18dc079/jbacter00191-0463-a.jpg

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Proteolysis in bacterial sporulation.细菌芽孢形成过程中的蛋白水解作用。
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Nutritional regulation of degradation of aspartate transcarbamylase and of bulk protein in exponentially growing Bacillus subtilis cells.指数生长的枯草芽孢杆菌细胞中天冬氨酸转氨甲酰酶及大量蛋白质降解的营养调控
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The mechanism of insertion of a segment of heterologous DNA into the chromosome of Bacillus subtilis.一段异源DNA片段插入枯草芽孢杆菌染色体的机制。
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