Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae

Pazehoski, Kristina O., Cobine, Paul A., Winzor, Donald J. and Dameron, Charles T. (2011) Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae. Biochemical and Biophysical Research Communications, 406 2: 183-187. doi:10.1016/j.bbrc.2011.01.118


Author Pazehoski, Kristina O.
Cobine, Paul A.
Winzor, Donald J.
Dameron, Charles T.
Title Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae
Formatted title
Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 0006-291X
1090-2104
Publication date 2011-03-11
Sub-type Article (original research)
DOI 10.1016/j.bbrc.2011.01.118
Open Access Status Not Open Access
Volume 406
Issue 2
Start page 183
End page 187
Total pages 5
Place of publication Philadelphia, United States
Publisher Elsevier
Language eng
Formatted abstract
Metal binding to the C-terminal region of the copper-responsive repressor protein CopY is responsible for homodimerization and the regulation of the copper homeostasis pathway in Enterococcus hirae. Specific involvement of the 38 C-terminal residues of CopY in dimerization is indicated by zonal and frontal (large zone) size-exclusion chromatography studies. The studies demonstrate that the attachment of these CopY residues to the immunoglobulin-binding domain of streptococcal protein G (GB1) promotes dimerization of the monomeric protein. Although sensitivity of dimerization to removal of metal from the fusion protein is smaller than that found for CopY (as measured by ultracentrifugation studies), the demonstration that an unrelated protein (GB1) can be induced to dimerize by extending its sequence with the C-terminal portion of CopY confirms the involvement of this region in CopY homodimerization.
Keyword Copper-responsive repressor protein
Frontal size-exclusion chromatography
Self-association stoichiometry
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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