CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase

Volume: 284, Issue: 19, Pages: 12735 - 12744
Published: May 1, 2009
Abstract
A new role is reported for CP12, a highly unfolded and flexible protein, mainly known for its redox function with A4 glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Both reduced and oxidized CP12 can prevent the in vitro thermal inactivation and aggregation of GAPDH from Chlamydomonas reinhardtii. This mechanism is thus not redox-dependent. The protection is specific to CP12, because other proteins, such as bovine serum albumin, thioredoxin,...
Paper Details
Title
CP12 from Chlamydomonas reinhardtii, a Permanent Specific “Chaperone-like” Protein of Glyceraldehyde-3-phosphate Dehydrogenase
Published Date
May 1, 2009
Volume
284
Issue
19
Pages
12735 - 12744
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