2 MAJOR PHOSPHOPROTEINS OF PLASMODIUM-FALCIPARUM ARE HEAT-SHOCK PROTEINS

Citation
B. Kappes et al., 2 MAJOR PHOSPHOPROTEINS OF PLASMODIUM-FALCIPARUM ARE HEAT-SHOCK PROTEINS, Molecular and biochemical parasitology, 59(1), 1993, pp. 83-94
Citations number
66
Categorie Soggetti
Parasitiology,Biology
ISSN journal
01666851
Volume
59
Issue
1
Year of publication
1993
Pages
83 - 94
Database
ISI
SICI code
0166-6851(1993)59:1<83:2MPOPA>2.0.ZU;2-9
Abstract
Two major phosphoproteins of Plasmodium falciparum could be identified by partial amino acid sequencing as the plasmodial members of the hsp 70 heat shock protein family, Pfhsp and Pfgrp. According to phosphoam ino acid analyses of Pfhsp and Pfgrp isolated from [P-32]orthophosphat e-labeled malarial cultures, both proteins were phosphorylated in Ser and Thr. While Pfhsp contains higher amounts of labeled phosphoserine, Pfgrp contains higher amounts of phosphothreonine. Phosphorylation of both proteins increased throughout the entire erythrocytic growth cyc le. At the trophozoite and schizont stages Pfhsp and Pfgrp are the mos t prominant phosphoproteins of Plasmodium falciparum. Using multiply r edundant oligonucleotides directed against the N-terminus of Pfgrp we cloned and sequenced the entire Pfgrp gene. The gene encodes a product with a predicted length of 652 amino acids. The deduced amino acid se quence has identities of 65.5% and 65.0% to the human and rat grp78 pr oteins, respectively. Pfgrp possesses a classical N-terminal leader se quence. The published grp78 related gene sequences of Plasmodium falci parum are all fragments of the same plasmodial gene.