Characterization of <Emphasis Type="Italic">Saccharomyces cerevisiae</Emphasis> protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Characterization of <Emphasis Type="Italic">Saccharomyces cerevisiae</Emphasis> protein Ser/Thr phosphatase T1 and comparison to its mammalian homolog PP5

Authors:	Jee-Yeong?Jeong Jeremiah?Johns Christopher?Sinclair Jung-Min?Park Email author" target="_blank">Sandra?Rossie Email author

Institution:	(1) Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA

Abstract:	Background Protein Ser/Thr phosphatase 5 (PP5) and its Saccharomyces cerevisiae homolog protein phosphatase T1 (Ppt1p) each contain an N-terminal domain consisting of several tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain that is related to the catalytic subunits of protein phosphatases 1 and 2A, and calcineurin. Analysis of yeast Ppt1p could provide important clues to the function of PP5 and its homologs, however it has not yet been characterized at the biochemical or cellular level.

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