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PP7, a plant phosphatase representing a novel evolutionary branch of eukaryotic protein Ser/Thr phosphatases
Author(s) -
Andreeva Alexandra V.,
Evans David E.,
Hawes Chris R.,
Bennett Nelly,
Kutuzov Mikhail A.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201752
Subject(s) - phosphatase , subfamily , arabidopsis thaliana , protein phosphatase 2 , arabidopsis , biology , acid phosphatase , microbiology and biotechnology , biochemistry , phosphorylation , enzyme , gene , mutant
We describe a novel protein Ser/Thr phosphatase from Arabidopsis thaliana, PP7, which is only 27‐32% identical in amino acid sequence to the known phosphatases and is the most divergent member of the PPP (PP1/2A/2B) family for today. Some structural features suggest more close relationship of PP7 to the PP5/rdgC subfamily. PP7 contains all of the residues essential for the phosphatase activity and possesses three major insertions in its presumable C‐terminal subdomain, which suggest its unique regulation and/or optimisation of its structure for interaction with specific substrates or regulators. A phosphatase structurally related to PP7 is expressed in rice. PP7 conservation between mono‐ and dicotyledonous plants may point to its essential role in the plant cell.