EXPRESSION OF ESCHERICHIA-COLI SECB IN BACILLUS-SUBTILIS FACILITATES SECRETION OF THE SECB-DEPENDENT MALTOSE-BINDING PROTEIN OF ESCHERICHIA-COLI

被引：12

作者：

COLLIER, DN

机构：

[1] Central Research/Development Div., E. I. DuPont de Nemours and Co., Experimental Station, Wilmington, DE 19880-0328

来源：

JOURNAL OF BACTERIOLOGY | 1994年 / 176卷 / 16期

关键词：

D O I：

10.1128/jb.176.16.4937-4940.1994

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Less than 20% of the Escherichia coli maltose-binding protein (MBP) synthesized in Bacillus subtilis is exported. However, a portion of the secreted MBP was processed cotranslationally. Coexpression of SecB, a secretion-related chaperone of E. coli, stimulated posttranslational export of MBP in B. subtilis but inhibited its cotranslational processing. Export of a SecB-independent MBP-ribose-binding protein hybrid precursor was not enhanced by SecB. A slowly folding MBP derivative (MBP-Y283D) was more efficiently secreted than wild-type MBP, suggesting that the antifolding activity of SecB promotes posttranslational secretion of MBP in B. subtilis.

引用

页码：4937 / 4940

页数：4

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