Plasmodium falciparum protein phosphatase type 1 functionally complements a glc7 mutant in Saccharomyces cerevisiae
International Journal for Parasitology
Calyculin A; Complementation; glc7; Hyperphosphorylation; Plasmodium falciparum; Protein phosphatase type 1; Saccharomyces cerevisiae
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 II 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. © 2002 Australian Society for Parasitology Inc. Published by Elsevier Science Ltd. All rights reserved.
Bhattacharyya, M., Hong, Z., Kongkasuriyachai, D., & Kumar, N. (2002). Plasmodium falciparum protein phosphatase type 1 functionally complements a glc7 mutant in Saccharomyces cerevisiae. International Journal for Parasitology, 32 (6). http://dx.doi.org/10.1016/S0020-7519(02)00007-3