KFU. Card publication. Различное влияние глутаминсинтетазы на ДНК-связывающую активность факторов транскрипции TnrA и GlnR из Bacillus subtilis.

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РАЗЛИЧНОЕ ВЛИЯНИЕ ГЛУТАМИНСИНТЕТАЗЫ НА ДНК-СВЯЗЫВАЮЩУЮ АКТИВНОСТЬ ФАКТОРОВ ТРАНСКРИПЦИИ TNRA И GLNR ИЗ BACILLUS SUBTILIS.

Form of presentation

Articles in Russian journals and collections

Year of publication

2013

Язык

русский

Authors, employees of KFU

Ilinskaya Olga Nikolaevna, author

Kayumov Ayrat Rashitovich, author

Sharafutdinov Irshad Sultanovich, author

Bibliographic description in the original language

K. P. Fedorova, I.S. Sharafutdinov, N.V. Tarasov, E.O.Mikhaylova, O. N. Ilinskaya, A. R. Kayumov Razlichnoe vliyanie glutaminsintetazy na DNK-svyazyvayushhuyu aktivnost faktorov transkripcii TnrA i GlnR iz Bacillus subtilis // Vestnik Kazanskogo tekhnologicheskogo universiteta. - 2013. – T.16. - №10. – S.198-200.

Annotation

The transcription factors TnrA and GlnR, members of the MerR family of transcription regulators, control the genes of the nitrogen metabolism in Bacillus subtilis under conditions of nitrogen deficiency and excess, respectively. Their DNA-binding activity is regulated by the interaction with the glutamine synthetase, the key enzyme of ammonium assimilation. By surface plasmon resonance it has been established that glutamine synthetase has a different effect on the activity of these transcription factors. In the presence of inhibited glutamine synthetase, the DNA-binding activity of TnrA is decreased, while GlnR affinity to DNA increases. This fact correlates with the activity of TnrA and GlnR in various conditions of nitrogen availability and characterizes the glutamine synthetase as a trigger enzyme that controls nitrogen metabolism.

Keywords

Bacillus subtilis, transcription factors TnrA and GlnR, glutamine synthetase.

The name of the journal

Вестник Казанского технологического университета

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

https://repository.kpfu.ru/eng/?p_id=88629&p_lang=2

Resource files

File name	Size (MB)	Format
BsGlnR.pdf	0,43	pdf	show / download

Full metadata record

Field DC	Value	Language
dc.contributor.author	Ilinskaya Olga Nikolaevna	ru_RU
dc.contributor.author	Kayumov Ayrat Rashitovich	ru_RU
dc.contributor.author	Sharafutdinov Irshad Sultanovich	ru_RU
dc.date.accessioned	2013-01-01T00:00:00Z	ru_RU
dc.date.available	2013-01-01T00:00:00Z	ru_RU
dc.date.issued	2013	ru_RU
dc.identifier.citation	К. П. Федорова, И.С. Шарафутдинов, Н.В. Тарасов, Е.О.Михайлова, О. Н. Ильинская, А. Р. Каюмов Различное влияние глутаминсинтетазы на ДНК-связывающую активность факторов транскрипции TnrA и GlnR из Bacillus subtilis // Вестник Казанского технологического университета. - 2013. – Т.16. - №10. – С.198-200.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=88629&p_lang=2	ru_RU
dc.description.abstract	Вестник Казанского технологического университета	ru_RU
dc.description.abstract	The transcription factors TnrA and GlnR, members of the MerR family of transcription regulators, control the genes of the nitrogen metabolism in Bacillus subtilis under conditions of nitrogen deficiency and excess, respectively. Their DNA-binding activity is regulated by the interaction with the glutamine synthetase, the key enzyme of ammonium assimilation. By surface plasmon resonance it has been established that glutamine synthetase has a different effect on the activity of these transcription factors. In the presence of inhibited glutamine synthetase, the DNA-binding activity of TnrA is decreased, while GlnR affinity to DNA increases. This fact correlates with the activity of TnrA and GlnR in various conditions of nitrogen availability and characterizes the glutamine synthetase as a trigger enzyme that controls nitrogen metabolism.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	Bacillus subtilis	ru_RU
dc.subject	transcription factors TnrA and GlnR	ru_RU
dc.subject	glutamine synthetase.	ru_RU
dc.title	Различное влияние глутаминсинтетазы на ДНК-связывающую активность факторов транскрипции TnrA и GlnR из Bacillus subtilis.	ru_RU
dc.type	Articles in Russian journals and collections	ru_RU