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New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent mannerстатья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 8 сентября 2020 г.
- Авторы: Semenyuk PI, Orlov VN, Sokolova OS, Kurochkina LP
- Журнал: Biochemical Journal
- Том: 473
- Номер: 15
- Год издания: 2016
- Издательство: Portland Press, Ltd.
- Местоположение издательства: United Kingdom
- Первая страница: 2383
- Последняя страница: 2393
- DOI: 10.1042/BCJ20160367
- Аннотация: Recently, we discovered and studied the first virus-encoded chaperonin of bacteriophage EL Pseudomonas aeruginosa, gene product (gp) 146. In the present work, we performed bioinformatics analysis of currently predicted GroEL-like proteins encoded by phage genomes in comparison with cellular and mitochondrial chaperonins. Putative phage chaperonins share a low similarity and do not form a monophyletic group; nevertheless, they are closer to bacterial chaperonins in the phylogenetic tree. Experimental investigation of putative GroEL-like chaperonin proteins has been continued by physicochemical and functional characterization of gp246 encoded by the genome of Pseudomonas fluorescens bacteriophage OBP. Unlike the more usual double-ring architecture of chaperonins, including the EL gp146, the recombinant gp246 produced by E. coli cells has been purified as a single heptameric ring. It possesses an ATPase activity and does not require a co-chaperonin for its functioning. In vitro experiments demonstrated that gp246 is able to suppress the thermal protein inactivation and aggregation in an ATP-dependent manner, thus indicating chaperonin function. Single particle electron microscopy analysis revealed the different conformational states of OBP chaperonin, depending on the bound nucleotide.
- Добавил в систему: Семенюк Павел Игоревич