Form of presentation | Conference proceedings in international journals and collections |
Year of publication | 2012 |
|
Kayumov Ayrat Rashitovich, author
|
Other authors |
K. Forchhammer |
Bibliographic description in the original language |
A.R. Kayumov, K. Forchhammer. The ATP binding properties of PII protein GlnK from Bacillus subtilis // Materialen des wissenschaftlichen Seminars von Stipendiaten der Programme "Michail Lomonosov II" und "Immanuel Kant II" 2011/12. Moskau, 28-29 April 2012. - S.63-66. |
Annotation |
The PII proteins are presented in almost all bacterial cells. In response lo ATP and 2-oxoglutatrate level in the cell Pll proteins regulates the activity of glutamine synthetase and activates the histidine kinase NtrB, which phosphorilates its cognate response regulator NtrC. The B.subtilis GlnK protein, although exhibiting unique features, was shown to bind to the membrane in an AmtB dependent manner and binds transcription factor TnrA. B.subtilis GlnK was shown to bind only ATP and not 2-oxoglutarate in contrast to other GlnK proteins. The point mutation Gly94 Ala abolishes ATP binding. In vivo, this protein is completely bound to membrane and not in a cytoplasm. This indicates that ATP is an intracellular signal regulating GlnK activity. |
Keywords |
B.subtilis, GlnK |
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=90498&p_lang=2 |
Full metadata record ![](https://shelly.kpfu.ru/pdf/picture/arrow_black_right.gif) |
Field DC |
Value |
Language |
dc.contributor.author |
Kayumov Ayrat Rashitovich |
ru_RU |
dc.date.accessioned |
2012-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2012-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2012 |
ru_RU |
dc.identifier.citation |
A.R. Kayumov, K. Forchhammer. The ATP binding properties of PII protein GlnK from Bacillus subtilis // Materialen des wissenschaftlichen Seminars von Stipendiaten der Programme "Michail Lomonosov II" und "Immanuel Kant II" 2011/12. Moskau, 28-29 April 2012. - S.63-66. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=90498&p_lang=2 |
ru_RU |
dc.description.abstract |
The PII proteins are presented in almost all bacterial cells. In response lo ATP and 2-oxoglutatrate level in the cell Pll proteins regulates the activity of glutamine synthetase and activates the histidine kinase NtrB, which phosphorilates its cognate response regulator NtrC. The B.subtilis GlnK protein, although exhibiting unique features, was shown to bind to the membrane in an AmtB dependent manner and binds transcription factor TnrA. B.subtilis GlnK was shown to bind only ATP and not 2-oxoglutarate in contrast to other GlnK proteins. The point mutation Gly94 Ala abolishes ATP binding. In vivo, this protein is completely bound to membrane and not in a cytoplasm. This indicates that ATP is an intracellular signal regulating GlnK activity. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
B.subtilis |
ru_RU |
dc.subject |
GlnK |
ru_RU |
dc.title |
The ATP binding properties of PII protein GlnK from Bacillus subtilis. |
ru_RU |
dc.type |
Conference proceedings in international journals and collections |
ru_RU |
|