CHLORAMPHENICOL ACETYLTRANSFERASE, A CYTOPLASMIC PROTEIN IS INCOMPATIBLE FOR EXPORT FROM BACILLUS-SUBTILIS

被引：7

作者：

CHEN, MW ^{[1
]}

NAGARAJAN, V ^{[1
]}

机构：

[1] DUPONT CO INC,DIV CENT RES & DEV,WILMINGTON,DE 19880

来源：

JOURNAL OF BACTERIOLOGY | 1993年 / 175卷 / 17期

关键词：

D O I：

10.1128/JB.175.17.5697-5700.1993

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Bacillus subtilis cells expressing a hybrid protein (Lvs(ss)-Cat) consisting of the B. amyloliquefaciens levansucrase signal peptide fused to B. pumilus chloramphenicol acetyltransferase (Cat) are unable to export Cat protein into the growth medium. A series of tripartite protein fusions was constructed by inserting various lengths of the Cat sequences between the levansucrase signal peptide and staphylococcal protein A or Escherichia coli alkaline phosphatase. Biochemical characterization of the various Cat protein fusions revealed that multiple regions in the Cat protein were causing the export defect.

引用

页码：5697 / 5700

页数：4

共 21 条

[11] MODULAR EXPRESSION AND SECRETION VECTORS FOR BACILLUS-SUBTILIS [J].