PHOSPHORYLATION OF MYCOPLASMA-PNEUMONIAE CYTADHERENCE-ACCESSORY PROTEINS IN CELL-EXTRACTS

被引：16

作者：

KREBES, KA ^{[1
]}

DIRKSEN, LB ^{[1
]}

KRAUSE, DC ^{[1
]}

机构：

[1] UNIV GEORGIA,DEPT MICROBIOL,ATHENS,GA 30602

来源：

JOURNAL OF BACTERIOLOGY | 1995年 / 177卷 / 15期

关键词：

D O I：

10.1128/jb.177.15.4571-4574.1995

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A cell-free system was used to characterize the phosphorylation of Mycoplasma pneumoniae proteins HMW1 acid HMW2, which are involved in the adherence of this organism to human tracheal epithelium during infection. The pH and cation requirements for phosphorylation of HMW1 and HMW2 were determined, and the effects of glycolytic intermediates, cyclic AMP, and eukaryotic kinase-phosphatase inhibitors and stimulators on this process were examined. Phosphoamino acid analysis identified serine as the major phosphate acceptor for both HMW1 and HMW2 in this system.

引用

页码：4571 / 4574

页数：4

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