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恶性疟原虫的两种主要磷蛋白是热休克蛋白。

Two major phosphoproteins of Plasmodium falciparum are heat shock proteins.

作者信息

Kappes B, Suetterlin B W, Hofer-Warbinek R, Humar R, Franklin R M

机构信息

Department of Structural Biology, University of Basel, Switzerland.

出版信息

Mol Biochem Parasitol. 1993 May;59(1):83-94. doi: 10.1016/0166-6851(93)90009-m.

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 phosphoamino acid analyses of Pfhsp and Pfgrp isolated from [32P]orthophosphate-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 cycle. At the trophozoite and schizont stages Pfhsp and Pfgrp are the most prominent phosphoproteins of Plasmodium falciparum. Using multiply redundant 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 sequence has identities of 65.5% and 65.0% to the human and rat grp78 proteins, respectively. Pfgrp possesses a classical N-terminal leader sequence. The published grp78 related gene sequences of Plasmodium falciparum are all fragments of the same plasmodial gene.

摘要

恶性疟原虫的两种主要磷蛋白经部分氨基酸测序可鉴定为热休克蛋白70(hsp 70)家族的疟原虫成员,即Pfhsp和Pfgrp。根据从[32P]正磷酸盐标记的疟原虫培养物中分离出的Pfhsp和Pfgrp的磷酸氨基酸分析,这两种蛋白在丝氨酸(Ser)和苏氨酸(Thr)处均被磷酸化。虽然Pfhsp含有较高量的标记磷酸丝氨酸,但Pfgrp含有较高量的磷酸苏氨酸。在整个红细胞生长周期中,这两种蛋白的磷酸化均增加。在滋养体和裂殖体阶段,Pfhsp和Pfgrp是恶性疟原虫最显著的磷蛋白。我们使用针对Pfgrp N端的多重冗余寡核苷酸克隆并测序了整个Pfgrp基因。该基因编码一个预测长度为652个氨基酸的产物。推导的氨基酸序列与人类和大鼠的grp78蛋白分别具有65.5%和65.0%的同源性。Pfgrp具有一个典型的N端前导序列。已发表的恶性疟原虫grp78相关基因序列均为同一疟原虫基因的片段。

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