当前位置： SCI文献检索 > PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA期刊下所有文献 > The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NIFL.

The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NIFL.

Abstract：

:The NIFA protein of Klebsiella pneumoniae is required for transcription of all nif (nitrogen fixation) operons except the regulatory nifLA operon itself. NIFA activates transcription of nif operons by the alternative holoenzyme form of RNA polymerase, sigma 54-holoenzyme, in a nucleoside triphosphate (NTP)-dependent manner. NIFL antagonizes the action of NIFA in the presence of molecular oxygen or combined nitrogen. The NIFA protein of K. pneumoniae is composed of three domains: an N-terminal domain with unclear function, a central catalytic domain, and a C-terminal DNA-binding domain. We report that the isolated central domain of NIFA activates transcription in vitro and that this activation requires NTP with a hydrolyzable beta-gamma bond, as does activation by intact NIFA. Transcriptional activation by the isolated central domain has the heat lability characteristic of intact NIFA and is inhibited by NIFL. The central domain has an NTPase activity that is also heat-labile but is not inhibited by NIFL. Taken together, these results imply that NIFL interferes with contact between NIFA and sigma 54-holoenzyme.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Berger DK,Narberhaus F,Kustu S

doi

10.1073/pnas.91.1.103

subject

Has Abstract

pub_date

1994-01-04 00:00:00

pages

103-7

issue

1

eissn

0027-8424

issn

1091-6490

journal_volume

91

pub_type

杂志文章

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