ESCHERICHIA-COLI CYCLIC-AMP RECEPTOR PROTEIN MUTANTS PROVIDE EVIDENCE FOR LIGAND CONTACTS IMPORTANT IN ACTIVATION

被引：26

作者：

MOORE, J

KANTOROW, M

VANDERZWAAG, D

MCKENNEY, K

机构：

[1] MARYLAND BIOTECHNOL INST,CTR ADV RES BIOTECHNOL,9600 GUDELSKY DR,ROCKVILLE,MD 20850

[2] NATL INST STAND & TECHNOL,ROCKVILLE,MD 20850

来源：

JOURNAL OF BACTERIOLOGY | 1992年 / 174卷 / 24期

关键词：

D O I：

10.1128/JB.174.24.8030-8035.1992

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The three-dimensional model of the Escherichia coli cyclic AMP (cAMP) receptor protein (CRP) shows that several amino acids are involved as chemical contacts for binding cAMP. We have constructed and characterized mutants at four of these positions, E72, R82, S83, and R123. The mutations were made in wild-type crp as well as a cAMP-independent crp, crp*. The activities of the mutant proteins were characterized in vivo for their ability to activate the lac operon. These results provide genetic evidence to support that E72 and R82 are essential and S83 and R123 are important in the activation of CRP by cAMP.

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页码：8030 / 8035

页数：6

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