Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein.

Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Research Abstract Details 

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Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Abstract Text:

Lewis V Wray,Susan H Fisher,

The Bacillus subtilis TnrA transcription factor belongs to the MerR family of proteins and regulates gene expression during nitrogen-limited growth. When B. subtilis cells are grown with excess nitrogen, feedback-inhibited glutamine synthetase forms a protein-protein complex with TnrA that prevents TnrA from binding to DNA. The C-terminal region of TnrA is required for the interaction with glutamine synthetase. Alanine scanning mutagenesis of the C-terminal region of TnrA identified three classes of mutants that altered the regulation by glutamine synthetase. While expression of the TnrA-regulated amtB gene was expressed constitutively in the class I (M96A, Q100A, and A103G) and class II (L97A, L101A, and F105A) mutants, the class II mutants were unable to grow on minimal medium unless a complex mixture of amino acids was present. The class III tnrA mutants (R93A, G99A, N102A, H104A, and Y107A mutants) were partially defective in the regulation of TnrA activity. In vitro experiments showed that feedback-inhibited glutamine synthetase had a significantly reduced ability to inhibit the DNA-binding activity of several class I and class II mutant TnrA proteins. A coiled-coil homology model of the C-terminal region of TnrA is used to explain the properties of the class I and II mutant proteins. The C-terminal region of TnrA corresponds to a dimerization domain in other MerR family proteins. Surprisingly, gel filtration and cross-linking analysis showed that a truncated TnrA protein which contained only the N-terminal DNA binding domain was dimeric. The implications of these results for the structure of TnrA are discussed.

Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Publishing Authors By Initials

LV Wray,SH Fisher,

For similar proteins: transcription factors research abstracts see: proteins: transcription factors research

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Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of bacteriology

VOLUME: 189

Page Numbers: 20-7

Journal Abbreviation: J. Bacteriol.

ISSN: 0021-9193

DAY: 3

MONTH: 11

YEAR: 2006

Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985120

Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Keywords Mesh Terms:

KEYWORDS: Transcription Factors

MESH TERMS: physiology

Chemical & Substance for Abstract: Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein. Information

Substance Name: Glutamate-Ammonia Ligase

Registry Number: EC 6.3.1.2

Grant and Affiliation Information for Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein.

AFFILIATION: Department of Microbiology, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118-2526, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM51127

ACRONYM: GM

MEDLINETA: J Bacteriol

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