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

Mrinal K. Bhattacharyya, Zheng Hong, Darin Kongkasuriyachai, Nirbhay Kumar

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)739-747
Number of pages9
JournalInternational Journal for Parasitology
Volume32
Issue number6
DOIs
StatePublished - 2002

Keywords

  • Calyculin A
  • Complementation
  • Hyperphosphorylation
  • Plasmodium falciparum
  • Protein phosphatase type 1
  • Saccharomyces cerevisiae
  • glc7

ASJC Scopus subject areas

  • Parasitology
  • Infectious Diseases

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