Oct, 2006
Contribution of the C-terminal region to the thermostability of the archaeal group II chaperonin from Thermococcus sp strain KS-1
EXTREMOPHILES
- ,
- ,
- ,
- ,
- ,
- ,
- ,
- Volume
- 10
- Number
- 5
- First page
- 451
- Last page
- 459
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1007/s00792-006-0519-y
- Publisher
- SPRINGER JAPAN KK
Chaperonin is a double ring-shaped oligomeric protein complex, which captures a protein in the folding intermediate state and assists its folding in an ATP-dependent manner. The chaperonin from a hyperthermophilic archaeum, Thermococcus sp. strain KS-1, is a group II chaperonin and is composed of two distinct subunits, alpha and beta. Although these subunits are highly homologous in sequence, the homo-oligomer of the beta-subunit is more thermostable than that of the alpha-subunit. To identify the region responsible for this difference in thermostability, we constructed domain-exchange mutants. The mutants containing the equatorial domain of the beta-subunit were more resistant to thermal dissociation than the mutants with that of the alpha-subunit. Thermostability of a beta-subunit mutant whose C-terminal 22 residues were replaced with those of the alpha-subunit decreased to the comparable level of that of the alpha-subunit homo-oligomer. These results indicate that the difference in thermostability between alpha and beta-subunits mainly originates in the C-terminal residues in the equatorial domain, only where they exhibit substantial sequence difference.
- Link information
-
- DOI
- https://doi.org/10.1007/s00792-006-0519-y
- CiNii Articles
- http://ci.nii.ac.jp/naid/80018879115
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/16685467
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000241861500011&DestApp=WOS_CPL
- ID information
-
- DOI : 10.1007/s00792-006-0519-y
- ISSN : 1431-0651
- CiNii Articles ID : 80018879115
- Pubmed ID : 16685467
- Web of Science ID : WOS:000241861500011