Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps.
The cytoplasmic chaperonin containing TCP-1 (CCT) plays a critically important role in the folding and biogenesis of many cytoskeletal proteins, including tubulin and actin. For marine ectotherms, the chronically cold Southern Ocean (-2 to +2 degrees C) poses energetic challenges to protein folding,...
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Language: | English |
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2006
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Online Access: | http://hdl.handle.net/11581/102220 https://doi.org/10.1007/s00792-006-0528-x |
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/102220 2023-05-15T13:39:10+02:00 Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. PUCCIARELLI, Sandra PARKER SK DETRICH HW RD MELKI R. Pucciarelli, Sandra Parker, Sk DETRICH HW, Rd Melki, R. 2006 http://hdl.handle.net/11581/102220 https://doi.org/10.1007/s00792-006-0528-x eng eng volume:10 issue:10 firstpage:537 lastpage:549 numberofpages:13 journal:EXTREMOPHILES http://hdl.handle.net/11581/102220 doi:10.1007/s00792-006-0528-x info:eu-repo/semantics/article 2006 ftuncamerinoiris https://doi.org/10.1007/s00792-006-0528-x 2023-03-01T21:03:32Z The cytoplasmic chaperonin containing TCP-1 (CCT) plays a critically important role in the folding and biogenesis of many cytoskeletal proteins, including tubulin and actin. For marine ectotherms, the chronically cold Southern Ocean (-2 to +2 degrees C) poses energetic challenges to protein folding, both at the level of substrate proteins and with respect to the chaperonin/chaperone folding system. Here we report the partial functional and structural characterization of CCT from an Antarctic notothenioid fish, Notothenia coriiceps. We find that the mechanism of folding by the Antarctic. sh CCT differed from that of mammalian CCT: (1) the former complex was able to bind denatured beta-tubulin but (2) when reconstituted with rabbit Cofactor A, failed to release the protein to yield the tubulin/cofactor intermediate. Moreover, the amino acid sequences of the N. coriiceps CCT beta and theta chains contained residue substitutions in the equatorial, apical, and intermediate domains that would be expected to increase the flexibility of the subunits, thus facilitating function of the chaperonin in an energy poor environment. Our work contributes to the growing realization that protein function in cold-adapted organisms reflects a delicate balance between the necessity of structural flexibility for catalytic activity and the concomitant hazard of cold-induced denaturation. Article in Journal/Newspaper Antarc* Antarctic Southern Ocean CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) Antarctic Southern Ocean The Antarctic Extremophiles 10 6 537 549 |
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Open Polar |
collection |
CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
op_collection_id |
ftuncamerinoiris |
language |
English |
description |
The cytoplasmic chaperonin containing TCP-1 (CCT) plays a critically important role in the folding and biogenesis of many cytoskeletal proteins, including tubulin and actin. For marine ectotherms, the chronically cold Southern Ocean (-2 to +2 degrees C) poses energetic challenges to protein folding, both at the level of substrate proteins and with respect to the chaperonin/chaperone folding system. Here we report the partial functional and structural characterization of CCT from an Antarctic notothenioid fish, Notothenia coriiceps. We find that the mechanism of folding by the Antarctic. sh CCT differed from that of mammalian CCT: (1) the former complex was able to bind denatured beta-tubulin but (2) when reconstituted with rabbit Cofactor A, failed to release the protein to yield the tubulin/cofactor intermediate. Moreover, the amino acid sequences of the N. coriiceps CCT beta and theta chains contained residue substitutions in the equatorial, apical, and intermediate domains that would be expected to increase the flexibility of the subunits, thus facilitating function of the chaperonin in an energy poor environment. Our work contributes to the growing realization that protein function in cold-adapted organisms reflects a delicate balance between the necessity of structural flexibility for catalytic activity and the concomitant hazard of cold-induced denaturation. |
author2 |
Pucciarelli, Sandra Parker, Sk DETRICH HW, Rd Melki, R. |
format |
Article in Journal/Newspaper |
author |
PUCCIARELLI, Sandra PARKER SK DETRICH HW RD MELKI R. |
spellingShingle |
PUCCIARELLI, Sandra PARKER SK DETRICH HW RD MELKI R. Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
author_facet |
PUCCIARELLI, Sandra PARKER SK DETRICH HW RD MELKI R. |
author_sort |
PUCCIARELLI, Sandra |
title |
Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
title_short |
Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
title_full |
Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
title_fullStr |
Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
title_full_unstemmed |
Characterization of the cytoplasmic chaperonin containing TCP-1 from the Antarctic fish Notothenia coriiceps. |
title_sort |
characterization of the cytoplasmic chaperonin containing tcp-1 from the antarctic fish notothenia coriiceps. |
publishDate |
2006 |
url |
http://hdl.handle.net/11581/102220 https://doi.org/10.1007/s00792-006-0528-x |
geographic |
Antarctic Southern Ocean The Antarctic |
geographic_facet |
Antarctic Southern Ocean The Antarctic |
genre |
Antarc* Antarctic Southern Ocean |
genre_facet |
Antarc* Antarctic Southern Ocean |
op_relation |
volume:10 issue:10 firstpage:537 lastpage:549 numberofpages:13 journal:EXTREMOPHILES http://hdl.handle.net/11581/102220 doi:10.1007/s00792-006-0528-x |
op_doi |
https://doi.org/10.1007/s00792-006-0528-x |
container_title |
Extremophiles |
container_volume |
10 |
container_issue |
6 |
container_start_page |
537 |
op_container_end_page |
549 |
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1766115382205087744 |