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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Public Library of Science (PLoS)
2014-01-01
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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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language | English |
last_indexed | 2024-12-10T06:41:03Z |
publishDate | 2014-01-01 |
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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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