Recently, we discovered and studied the first virus-encoded chaperonin of bacteriophage EL Pseudomonas aeruginosa, gene product (gp) 146. In the present study, 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 Escherichia coli cells has been purified as a single heptameric ring. It possesses ATPase activity and does not require a co-chaperonin for its function. 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.
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Research Article|
July 28 2016
New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner
Pavel I. Semenyuk
;
Pavel I. Semenyuk
1
*
Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia1
To whom correspondence should be addressed (email psemenyuk@belozersky.msu.ru).
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Victor N. Orlov
;
Victor N. Orlov
*
Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia
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Olga S. Sokolova
;
Olga S. Sokolova
†
Department of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia
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Lidia P. Kurochkina
Lidia P. Kurochkina
*
Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, Russia‡
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
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Biochem J (2016) 473 (15): 2383-2393.
Article history
Received:
April 20 2016
Revision Received:
May 10 2016
Accepted:
May 31 2016
Accepted Manuscript online:
June 01 2016
Citation
Pavel I. Semenyuk, Victor N. Orlov, Olga S. Sokolova, Lidia P. Kurochkina; New GroEL-like chaperonin of bacteriophage OBP Pseudomonas fluorescens suppresses thermal protein aggregation in an ATP-dependent manner. Biochem J 1 August 2016; 473 (15): 2383–2393. doi: https://doi.org/10.1042/BCJ20160367
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