Title of article
Purification of Plant Protein Phosphatase PP7 and Evidence for Its Redox Regulation
Author/Authors
Andreeva، نويسنده , , Alexandra V. and Solovʹeva، نويسنده , , Olga V. and Kakuev، نويسنده , , Dmitry L. and Kutuzov، نويسنده , , Mikhail A.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2001
Pages
6
From page
65
To page
70
Abstract
PP7, a recently identified protein Ser/Thr phosphatase of the PPP family distantly related to phosphatases PP5/PPT and PPEF/rdgC, was purified from cauliflower extracts to apparent homogeneity. Purified cauliflower PP7 and recombinant PP7 expressed in Escherichia coli exhibit light absorption in the visible range with a maximum at ∼430 nm. Under nonreducing conditions, native PP7 exists as a mixture of monomer with an intramolecular disulfide bridge, disulfide-linked homodimer, and possibly disulfide-linked complexes with potential partner proteins. The activity of recombinant Arabidopsis thaliana PP7 is reversibly regulated by redox agents. The results demonstrate the existence of PP7 protein in planta and suggest a possibility of redox regulation of this protein phosphatase.
Keywords
protein phosphorylation , protein Ser/Thr phosphatase , PP7 , Purification , redox , thiol-disulfide exchange , Arabidopsis thaliana.
Journal title
Archives of Biochemistry and Biophysics
Serial Year
2001
Journal title
Archives of Biochemistry and Biophysics
Record number
1618789
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