Expression, purification, and functional analysis of the C-terminal domain of Herbaspirillum seropedicae NifA protein

被引：8

作者：

Monteiro, RA ^{[1
]}

Souza, EM ^{[1
]}

Yates, MG ^{[1
]}

Steffens, MBR ^{[1
]}

Pedrosa, FO ^{[1
]}

Chubatsu, LS ^{[1
]}

机构：

[1] Univ Fed Parana, Dept Biochem & Mol Biol, BR-81531990 Curitiba, Parana, Brazil

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2003年 / 27卷 / 02期

关键词：

Herbaspirillum seropedicae; NifA protein; transcriptional activator; nitrogen fixation;

D O I：

10.1016/S1046-5928(02)00635-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The Herbaspirillum seropedicae NifA protein is responsible for nif gene expression. The C-terminal domain of the H. seropedicae NifA protein, fused to a His-Tag sequence (His-Tag-C-terminal), was over-expressed and purified by metal-affinity chromatography to yield a highly purified and active protein. Band-shift assays showed that the NifA His-Tag-C-terminal bound specifically to the H. seropedicae nifB promoter region in vitro. In vivo analysis showed that this protein inhibited the Central + C-terminal domains of NifA protein from activating the nifH promoter of K pneumoniae in Escherichia coli, indicating that the protein must be bound to the NifA-binding site (UAS site) at the nifH promoter region to activate transcription. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：313 / 318

页数：6

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