EXPRESSION IN ESCHERICHIA-COLI OF THE CARBOXY TERMINAL DOMAIN OF THE BLAR SENSORY-TRANSDUCER PROTEIN OF BACILLUS-LICHENIFORMIS AS A WATER-SOLUBLE MR-26000 PENICILLIN-BINDING PROTEIN

被引：30

作者：

JORIS, B

LEDENT, P

KOBAYASHI, T

LAMPEN, JO

GHUYSEN, JM

机构：

[1] UNIV LIEGE, INST CHIM, SERV MICROBIOL, B6, B-4000 Sart Tilman Par Liege 1, BELGIUM

[2] RUTGERS STATE UNIV, WAKSMAN INST MICROBIOL, NEW BRUNSWICK, NJ 08903 USA

来源：

FEMS MICROBIOLOGY LETTERS | 1990年 / 70卷 / 01期

关键词：

Bacillus licheniformis; BLAR-CTD; Escherichia coli; ß-Lactamase induction;

D O I：

10.1016/0378-1097(90)90111-3

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A cloning vector has been constructed which allows production and export by Escherichia coli of the Met346-Arg601 carboxy terminal domain of the 601 aminoc acid BLAR sensory-transducer involved in ß-lactamase inducibility in Bacillus Licheniformis. The polypeptide, referred to as BLAR-CTD, accumulates in the periplasm of E. coli in the form of a water-soluble, Mr 26 000 penicillin-binding protein. These data and homology searches suggest that BLAR has a membrane topology similar to that of other sensory-transducers involved in chemotaxis. © 1990.

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页码：107 / 113

页数：7

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