The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.

The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro. In the current work, we present data on the structure and function of the third A. thaliana co-chaperonin, whi...

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Main Authors: Anna Vitlin Gruber, Gal Zizelski, Abdussalam Azem, Celeste Weiss
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4242682?pdf=render
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author Anna Vitlin Gruber
Gal Zizelski
Abdussalam Azem
Celeste Weiss
author_facet Anna Vitlin Gruber
Gal Zizelski
Abdussalam Azem
Celeste Weiss
author_sort Anna Vitlin Gruber
collection DOAJ
description The A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro. In the current work, we present data on the structure and function of the third A. thaliana co-chaperonin, which exhibits unique properties. We found that purified recombinant Cpn10(1) forms inactive dimers in solution, in contrast to the active heptamers that are formed by canonical Cpn10s. Additionally, our data demonstrate that Cpn10(1) is capable of assembling into active hetero-oligomers together with Cpn20. This finding was reinforced by the formation of active co-chaperonin species upon mixing an inactive Cpn20 mutant with the inactive Cpn10(1). The present study constitutes the first report of a higher plant Cpn10 subunit that is able to function only upon formation of hetero-oligomers with other co-chaperonins.
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spelling doaj.art-2f3c28160d1149d093c748db59487fd72022-12-22T01:58:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-01911e11383510.1371/journal.pone.0113835The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.Anna Vitlin GruberGal ZizelskiAbdussalam AzemCeleste WeissThe A. thaliana genome encodes five co-chaperonin homologs, three of which are destined to the chloroplast. Two of the proteins, Cpn10(2) and Cpn20, form functional homo-oligomers in vitro. In the current work, we present data on the structure and function of the third A. thaliana co-chaperonin, which exhibits unique properties. We found that purified recombinant Cpn10(1) forms inactive dimers in solution, in contrast to the active heptamers that are formed by canonical Cpn10s. Additionally, our data demonstrate that Cpn10(1) is capable of assembling into active hetero-oligomers together with Cpn20. This finding was reinforced by the formation of active co-chaperonin species upon mixing an inactive Cpn20 mutant with the inactive Cpn10(1). The present study constitutes the first report of a higher plant Cpn10 subunit that is able to function only upon formation of hetero-oligomers with other co-chaperonins.http://europepmc.org/articles/PMC4242682?pdf=render
spellingShingle Anna Vitlin Gruber
Gal Zizelski
Abdussalam Azem
Celeste Weiss
The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
PLoS ONE
title The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
title_full The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
title_fullStr The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
title_full_unstemmed The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
title_short The Cpn10(1) co-chaperonin of A. thaliana functions only as a hetero-oligomer with Cpn20.
title_sort cpn10 1 co chaperonin of a thaliana functions only as a hetero oligomer with cpn20
url http://europepmc.org/articles/PMC4242682?pdf=render
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