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
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
UR - http://www.scopus.com/inward/record.url?scp=0036231626&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036231626&partnerID=8YFLogxK
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 -