KFU. Card publication. The ATP binding properties of PII protein GlnK from Bacillus subtilis.

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FEDERAL UNIVERSITY

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THE ATP BINDING PROPERTIES OF PII PROTEIN GLNK FROM BACILLUS SUBTILIS.

Form of presentation

Conference proceedings in international journals and collections

Year of publication

2012

Authors, employees of KFU

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

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