KFU. Card publication. The molecular basis of TnrA control by glutamine synthetase in Bacillus subtilis

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THE MOLECULAR BASIS OF TNRA CONTROL BY GLUTAMINE SYNTHETASE IN BACILLUS SUBTILIS

Form of presentation

Articles in international journals and collections

Year of publication

2015

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Authors, employees of KFU

Kayumov Ayrat Rashitovich, author

Other authors

Forchhammer Karl -, author

Gloge Felix -, author

Hauf Ksenia -, author

Bibliographic description in the original language

Hauf K. The molecular basis of TnrA control by glutamine synthetase in Bacillus subtilis / K.Hauf, A. Kayumov, Felix Gloge, Karl Forchhammer // Journal of biological chemistry. - 2015. - Vol.12.

Annotation

TnrA is a master regulator of nitrogen assimilation in Bacillus subtilis. This study focuses on the mechanism of how glutamine synthetase (GS) inhibits TnrA function in response to key metabolites ATP, AMP, glutamine and glutamate. We suggest a model of two mutually exclusive GS conformations governing the interaction with TnrA. In the ATP-bound state (A-state), GS is catalytically active, but unable to interact with TnrA. This conformation was stabilized by phosphorylated MSX, fixing the enzyme in the transition state. When occupied by glutamine (or its analogue MSX), GS resides in a conformation that has high affinity for TnrA (Q-state). The A- and Q-state are mutually exclusive and in agreement, ATP and glutamine bind to GS in a competitive manner. At elevated concentrations of glutamine, ATP is no more able to bind GS and to bring it into the A-state. AMP efficiently competes with ATP and prevents formation of the A-state, thereby favoring GS-TnrA interaction. SPR analysis shows th

Keywords

transcription factor TnrA, glutamine synthetase, transcription regulation, AMP, glutamine, glutamate, ATP, Bacillus subtilis

The name of the journal

JOURNAL OF BIOLOGICAL CHEMISTRY

URL

http://www.jbc.org/content/early/2015/12/03/jbc.M115.680991.abstract

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=121548&p_lang=2

Resource files

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J._Biol._Chem._2015.pdf	1,58	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.contributor.author	Forchhammer Karl -	ru_RU
dc.contributor.author	Gloge Felix -	ru_RU
dc.contributor.author	Hauf Ksenia -	ru_RU
dc.date.accessioned	2015-01-01T00:00:00Z	ru_RU
dc.date.available	2015-01-01T00:00:00Z	ru_RU
dc.date.issued	2015	ru_RU
dc.identifier.citation	Hauf K. The molecular basis of TnrA control by glutamine synthetase in Bacillus subtilis / K.Hauf, A. Kayumov, Felix Gloge, Karl Forchhammer // Journal of biological chemistry. - 2015. - Vol.12.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=121548&p_lang=2	ru_RU
dc.description.abstract	JOURNAL OF BIOLOGICAL CHEMISTRY	ru_RU
dc.description.abstract	TnrA is a master regulator of nitrogen assimilation in Bacillus subtilis. This study focuses on the mechanism of how glutamine synthetase (GS) inhibits TnrA function in response to key metabolites ATP, AMP, glutamine and glutamate. We suggest a model of two mutually exclusive GS conformations governing the interaction with TnrA. In the ATP-bound state (A-state), GS is catalytically active, but unable to interact with TnrA. This conformation was stabilized by phosphorylated MSX, fixing the enzyme in the transition state. When occupied by glutamine (or its analogue MSX), GS resides in a conformation that has high affinity for TnrA (Q-state). The A- and Q-state are mutually exclusive and in agreement, ATP and glutamine bind to GS in a competitive manner. At elevated concentrations of glutamine, ATP is no more able to bind GS and to bring it into the A-state. AMP efficiently competes with ATP and prevents formation of the A-state, thereby favoring GS-TnrA interaction. SPR analysis shows th	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	transcription factor TnrA	ru_RU
dc.subject	glutamine synthetase	ru_RU
dc.subject	transcription regulation	ru_RU
dc.subject	AMP	ru_RU
dc.subject	glutamine	ru_RU
dc.subject	glutamate	ru_RU
dc.subject	ATP	ru_RU
dc.subject	Bacillus subtilis	ru_RU
dc.title	The molecular basis of TnrA control by glutamine synthetase in Bacillus subtilis	ru_RU
dc.type	Articles in international journals and collections	ru_RU