|
|||||
|
|
Evidence for involvement of the C-terminal domain in the dimerization of the CopY repressor protein from Enterococcus hirae |
|
| Authors: | Pazehoski Kristina O Cobine Paul A Winzor Donald J Dameron Charles T |
| Affiliation: | aDivision of Natural Sciences, University of Pittsburgh at Greensburg, Greensburg, PA 15601, USA;bDepartment of Biological Sciences, 101 Rouse Life Science Building, Auburn University, AL 36849, USA;cDepartment of Biochemistry, University of Queensland, Brisbane, Queensland 4072, Australia;dDepartment of Chemistry, Saint Francis University, Loretto, PA 15940, USA |
| 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. |
| Keywords: | Abbreviations: CopY, copper-responsive repressor protein from Enterococcus hirae ESI mass spectrometry, electrospray ionization mass spectrometry GB1, immunoglobulin binding domain of streptococcal protein G Ymbs38, the 38 C-terminal residues comprising the metal-binding site region of CopY |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ | |