View : 23 Download: 4

Tetramerization Reinforces the Dimer Interface of MnSOD

Title
Tetramerization Reinforces the Dimer Interface of MnSOD
Authors
Sheng Y.Durazo A.Schumacher M.Gralla E.B.Cascio D.Cabelli D.E.Valentine J.S.
Ewha Authors
Joan S. Valentine
SCOPUS Author ID
Joan S. Valentinescopus
Issue Date
2013
Journal Title
PLoS ONE
ISSN
1932-6203JCR Link
Citation
vol. 8, no. 5
Indexed
SCIE; SCOPUS WOS scopus
Abstract
Two yeast manganese superoxide dismutases (MnSOD), one from Saccharomyces cerevisiae mitochondria (ScMnSOD) and the other from Candida albicans cytosol (CaMnSODc), have most biochemical and biophysical properties in common, yet ScMnSOD is a tetramer and CaMnSODc is a dimer or "loose tetramer" in solution. Although CaMnSODc was found to crystallize as a tetramer, there is no indication from the solution properties that the functionality of CaMnSODc in vivo depends upon the formation of the tetrameric structure. To elucidate further the functional significance of MnSOD quaternary structure, wild-type and mutant forms of ScMnSOD (K182R, A183P mutant) and CaMnSODc (K184R, L185P mutant) with the substitutions at dimer interfaces were analyzed with respect to their oligomeric states and resistance to pH, heat, and denaturant. Dimeric CaMnSODc was found to be significantly more subject to thermal or denaturant-induced unfolding than tetrameric ScMnSOD. The residue substitutions at dimer interfaces caused dimeric CaMnSODc but not tetrameric ScMnSOD to dissociate into monomers. We conclude that the tetrameric assembly strongly reinforces the dimer interface, which is critical for MnSOD activity. © 2013 Sheng et al.
DOI
10.1371/journal.pone.0062446
Appears in Collections:
일반대학원 > 바이오융합과학과 > Journal papers
Files in This Item:
Tetramerization Reinforces the Dimer Interface of MnSOD.PDF(882.36 kB)Download
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE