Form of presentation | Articles in international journals and collections |
Year of publication | 2008 |
|
Ilinskaya Olga Nikolaevna, author
Kayumov Ayrat Rashitovich, author
Sharipova Margarita Rashidovna, author
|
Other authors |
Karl Forchhamer; Annette Heinrich |
Bibliographic description in the original language |
A. Kayumov, A. Heinrich, M. Sharipova, O. Iljinskaya, K. Forchhammer. Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis // Microbiology. - 2008. - V.154. - P.2348-2355. DOI 10.1099/mic.0.2008/019802-0. |
Annotation |
Under conditions of nitrogen limitation, the general transcription factor TnrA in Bacillus subtilis activates the expression of genes involved in assimilation of various nitrogen sources. Previously, TnrA activity has been shown to be controlled by protein-protein interaction with glutamine synthetase, the key enzyme of ammonia assimilation. Furthermore, depending on ATP and 2-oxoglutarate levels, TnrA can bind to the GlnK-AmtB complex. Here, we report that upon transfer of nitrate-grown ceils to combined nitrogen-depleted medium, TnrA is rapidly eliminated from the cells by proteolysis. As long as TnrA is membrane-bound through GlnK-AmtB interaction it seems to be protected from degradation. Upon removal of nitrogen sources, the localization of TnrA becomes cytosolic and degradation occurs. The proteolytic activity against TnrA was detected in the cytosolic fraction but not in the membrane, and its presence does not depend on the nitrogen regime of cell growth. The proteolytic degradation of TnrA as a response to complete nitrogen starvation might represent a novel mechanism of TnrA control in B. subtilis. |
Keywords |
Bacillus subtilis, transcription factor TnrA. |
The name of the journal |
MICROBIOL-SGM
|
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=24078&p_lang=2 |
Resource files | |
|
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 |
Sharipova Margarita Rashidovna |
ru_RU |
dc.date.accessioned |
2008-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2008-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2008 |
ru_RU |
dc.identifier.citation |
A. Kayumov, A. Heinrich, M. Sharipova, O. Iljinskaya, K. Forchhammer. Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis // Microbiology. - 2008. - V.154. - P.2348-2355. DOI 10.1099/mic.0.2008/019802-0. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/eng/?p_id=24078&p_lang=2 |
ru_RU |
dc.description.abstract |
MICROBIOL-SGM |
ru_RU |
dc.description.abstract |
Under conditions of nitrogen limitation, the general transcription factor TnrA in Bacillus subtilis activates the expression of genes involved in assimilation of various nitrogen sources. Previously, TnrA activity has been shown to be controlled by protein-protein interaction with glutamine synthetase, the key enzyme of ammonia assimilation. Furthermore, depending on ATP and 2-oxoglutarate levels, TnrA can bind to the GlnK-AmtB complex. Here, we report that upon transfer of nitrate-grown ceils to combined nitrogen-depleted medium, TnrA is rapidly eliminated from the cells by proteolysis. As long as TnrA is membrane-bound through GlnK-AmtB interaction it seems to be protected from degradation. Upon removal of nitrogen sources, the localization of TnrA becomes cytosolic and degradation occurs. The proteolytic activity against TnrA was detected in the cytosolic fraction but not in the membrane, and its presence does not depend on the nitrogen regime of cell growth. The proteolytic degradation of TnrA as a response to complete nitrogen starvation might represent a novel mechanism of TnrA control in B. subtilis. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Bacillus subtilis |
ru_RU |
dc.subject |
transcription factor TnrA. |
ru_RU |
dc.title |
Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis. |
ru_RU |
dc.type |
Articles in international journals and collections |
ru_RU |
|