| Форма представления | Статьи в зарубежных журналах и сборниках |
| Год публикации | 2015 |
| Язык | английский |
|
Каюмов Айрат Рашитович, автор
|
|
Forchhammer Karl -, автор
Gloge Felix -, автор
Hauf Ksenia -, автор
|
| Библиографическое описание на языке оригинала |
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. |
| Аннотация |
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 |
| Ключевые слова |
transcription factor TnrA, glutamine synthetase, transcription regulation, AMP, glutamine, glutamate, ATP, Bacillus subtilis |
| Название журнала |
JOURNAL OF BIOLOGICAL CHEMISTRY
|
| URL |
http://www.jbc.org/content/early/2015/12/03/jbc.M115.680991.abstract |
| Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=121548 |
| Файлы ресурса | |
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Полная запись метаданных  |
| Поле DC |
Значение |
Язык |
| dc.contributor.author |
Каюмов Айрат Рашитович |
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/?p_id=121548 |
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 |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|
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