Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis

Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and euk...

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Published inBiomedicines Vol. 10; no. 10; p. 2347
Main Authors Sokolova, Olga S., Pichkur, Evgeny B., Maslova, Ekaterina S., Kurochkina, Lidia P., Semenyuk, Pavel I., Konarev, Petr V., Samygina, Valeriya R., Stanishneva-Konovalova, Tatiana B.
Format Journal Article
LanguageEnglish
Published Basel MDPI AG 21.09.2022
MDPI
Subjects
bacteriophages
Chaperonins
Cryo-EM
Cytosol
E coli
Genomes
molecular chaperones
Organelles
Phages
Protein folding
Symmetry
United States > US
Sweden
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Summary:Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and eukaryotes. Recently, chaperonins of a prospective new group were discovered in giant bacteriophages; however, structures have been determined for only two of them. Here, using cryo-EM, we resolved a structure of a new chaperonin encoded by gene 228 of phage AR9 B. subtilis. This structure has similarities and differences with members of both groups, as well as with other known phage chaperonins, which further proves their diversity.
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ISSN:2227-9059
2227-9059
DOI:10.3390/biomedicines10102347