TY - JOUR
T1 - Plasmodium falciparum protein phosphatase type 1 functionally complements a glc7 mutant in Saccharomyces cerevisiae
AU - Bhattacharyya, Mrinal K.
AU - Hong, Zheng
AU - Kongkasuriyachai, Darin
AU - Kumar, Nirbhay
N1 - Funding Information:
This work was supported by NIH grant AI46760. Supply of human erythrocyte for malaria culture is supported by NCCR OPD-GCRC RR00722. D.K. is supported by an NIH training grant. We are grateful to Prof. Kelly Tatchell for the generous gift of KT1704 strain of S. cerevisiae and valuable discussions. We are also indebted to Prof. Jeff Boeke for the gift of pADNS plasmid and the yeast strain BY4741.
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
KW - Calyculin A
KW - Complementation
KW - Hyperphosphorylation
KW - Plasmodium falciparum
KW - Protein phosphatase type 1
KW - Saccharomyces cerevisiae
KW - glc7
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U2 - 10.1016/S0020-7519(02)00007-3
DO - 10.1016/S0020-7519(02)00007-3
M3 - Article
C2 - 12062492
AN - SCOPUS:0036231626
VL - 32
SP - 739
EP - 747
JO - International Journal for Parasitology
JF - International Journal for Parasitology
SN - 0020-7519
IS - 6
ER -