用于SOS诱变的UmuD和MucA蛋白的蛋白水解激活。

Proteolytic activation of UmuD and MucA proteins for SOS mutagenesis.

作者信息

Shiba T, Iwasaki H, Nakata A, Shinagawa H

机构信息

Department of Experimental Chemotherapy, Osaka University, Japan.

出版信息

Basic Life Sci. 1990;52:351-4. doi: 10.1007/978-1-4615-9561-8_31.

DOI:10.1007/978-1-4615-9561-8_31

PMID:2183775

Abstract

SOS mutagenesis in Escherichia coli requires the functions of the umuD, C genes, or their functional analogues mucA, B derived from a plasmid pKM101, and the recA gene. However, mere derepression of these SOS genes does not increase the ability of the cell to perform mutagenesis. Activation of RecA protein to a form (RecA*) that mediates cleavage of the LexA repressor is required for mutagenesis. We present evidence that UmuD and MucA are proteolytically processed by RecA* and that the processed products are the active forms involved in mutagenesis.

摘要

大肠杆菌中的SOS诱变需要umuD、C基因的功能，或其来自质粒pKM101的功能类似物mucA、B以及recA基因的功能。然而，仅仅这些SOS基因的去阻遏并不会增加细胞进行诱变的能力。诱变需要将RecA蛋白激活为介导LexA阻遏物裂解的形式（RecA*）。我们提供的证据表明，UmuD和MucA被RecA*进行蛋白水解加工，且加工产物是参与诱变的活性形式。