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On the involvement of the regulatory gene prqR in the development of resistance to methyl viologen in cyanobacterium Synechocystis sp. PCC6803статья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Babykin M.M., Sidoruk K.V., Zinchenko V.V., Nefedova L.N., Cerff R., Shestakov S.V.
- Журнал: Genetika
- Том: 39
- Номер: 1
- Год издания: 2003
- Издательство: Izdatel'stva Nauka
- Местоположение издательства: Russian Federation
- Первая страница: 25
- Последняя страница: 32
- Аннотация: The role of the prqR gene in the regulation of the adaptive response of the cyanobacterium Synechocystis sp. PCC6803 to the oxidative stress induced with methyl viologen (MV) was studied. For this, transcription activity of prqR and the genes, which may be involved in the control of resistance to MV, was determined by means of Northern blot hybridization in wild-type cells and in the MV-resistant Prq20 mutant with a mutation located in the DNA-binding domain of the PrqR protein. It was ascertained that the prqR gene is a component of the prqR-prqA operon and down regulates its transcription. In cells of the wild-type strain containing MV, the autorepressor activity of the PrqR protein enhances and transcription of mvrA and sodB genes encoding an respectively assumed transporter protein and iron-containing superoxide dismutase increases. The prqR gene may be involved in the negative, indirect control of transcription of these genes. The Prq20 mutant is characterized by an MV-independent derepression of the prqR-prqA operon and by a slightly increased transcription of mvrA and sodB genes not stimulated by MV. Nevertheless, the expression of mvrA and sodB genes was lower than in wild-type cells after the MV treatment. On the strength of this evidence, it is assumed that the main mechanism underlying for the resistance to MV in the Prq20 mutant is derepression of the prqA gene, the product of which is homologous to multidrug transporters, drug efflux proteins.
- Добавил в систему: Зинченко Владислав Владимирович