嗜碱芽孢杆菌青霉素酶在大肠杆菌细胞质中的信号序列内被切割后的积累。

Accumulation of alkaliphilic Bacillus penicillinase cleaved within the signal sequence in cytoplasm of Escherichia coli.

作者信息

Aono R

机构信息

Department of Bioengineering, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.

出版信息

Biosci Biotechnol Biochem. 1992 Jun;56(6):890-5. doi: 10.1271/bbb.56.890.

DOI:10.1271/bbb.56.890

PMID:1369375

Abstract

Alkaliphilic Bacillus penicillinase produced by Escherichia coli is distributed in several subcellular compartments according to cultivation conditions. The penicillinase that accumulated in particular subcellular fractions of E. coli grown under different conditions was purified and characterized. Periplasmic or extracellular penicillinase (24 kDa) was mature protein, indicating that the putative precursor (27 kDa) was processed at the correct amino acid residue, probably by signal peptidase I. Cytoplasmic penicillinase contained two unusual proteins (25 kDa) that are produced by proteolytic cleavage of the precursor within its signal sequence.

摘要

由大肠杆菌产生的嗜碱芽孢杆菌青霉素酶根据培养条件分布在几个亚细胞区室中。对在不同条件下生长的大肠杆菌特定亚细胞组分中积累的青霉素酶进行了纯化和表征。周质或细胞外青霉素酶（24 kDa）是成熟蛋白，这表明假定的前体（27 kDa）可能由信号肽酶I在正确的氨基酸残基处进行了加工。细胞质青霉素酶包含两种异常蛋白（25 kDa），它们是由前体在其信号序列内的蛋白水解切割产生的。