Plasmodium falciparum protein phosphatase type 1 functionally complements a glc7 mutant in Saccharomyces cerevisiae

被引：30

作者：

Bhattacharyya, MK ^{[1
]}

Hong, Z ^{[1
]}

Kongkasuriyachai, D ^{[1
]}

Kumar, N ^{[1
]}

机构：

[1] Johns Hopkins Univ, Bloomberg Sch Publ Hlth, W Harry Feinstone Dept Mol Microbiol & Immunol, Malaria Res Inst, Baltimore, MD 21205 USA

来源：

INTERNATIONAL JOURNAL FOR PARASITOLOGY | 2002年 / 32卷 / 06期

关键词：

protein phosphatase type 1; Plasmodium falciparum; glc7; Saccharomyces cerevisiae; complementation; calyculin A; hyperphosphorylation;

D O I：

10.1016/S0020-7519(02)00007-3

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

We have identified a new homologue of protein phosphatase type 1 from Plasmodium falciparum, designated PfPP1, which shows 83-87% sequence identity with yeast and mammalian PP1s at the amino acid level. The PfPP1 sequence is strikingly different from all other P. falciparum Ser/Thr phosphatases cloned so far. The deduced 304 amino acid sequence revealed the signature sequence of Ser/Thr phosphatase LRGNHE, and two putative protein kinase C and five putative casein kinase 11 phosphorylation sites. Calyculin A, a potent inhibitor of Ser/Thr phosphatase 1 and 2A showed hyperphosphorylation of a 51 kDa protein among other parasite proteins. Okadaic acid on the other hand, was without any effect suggesting that PP1 activity might predominate over PP2A activity in intra-erythrocytic P. falciparum. Complementation studies showed that PfPP1 could rescue low glycogen phenotype of Saccharomyces cerevisiae glc7 (PP1(-)) mutant, strongly suggesting functional interaction of PfPP1 and yeast proteins involved in glycogen metabolism. (C) 2002 Australian Society for Parasitology Inc. Published by Elsevier Science Ltd. All rights reserved.

引用

页码：739 / 747

页数：9

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