ON THE POSTTRANSLATIONAL MODIFICATIONS AT THE C-TERMINAL DOMAIN OF THE MAJOR CYSTEINE PROTEINASE (CRUZIPAIN) FROM TRYPANOSOMA-CRUZI

被引：29

作者：

CAZZULO, JJ ^{[1
]}

MARTINEZ, J ^{[1
]}

PARODI, AJA ^{[1
]}

WERNSTEDT, C ^{[1
]}

HELLMAN, U ^{[1
]}

机构：

[1] LUDWIG INST CANC RES,UPPSALA BRANCH,UPPSALA,SWEDEN

来源：

FEMS MICROBIOLOGY LETTERS | 1992年 / 100卷 / 1-3期

关键词：

TRYPANOSOMA-CRUZI; CYSTEINE PROTEINASE; PROTEINASE; POSTTRANSLATIONAL MODIFICATION; CRUZIPAIN;

D O I：

10.1111/j.1574-6968.1992.tb05733.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Cruzipain, the major cysteine proteinase from Trypanosoma cruzi, has a 130 amino acid-long C-terminal domain, which, although microheterogeneous in SDS-PAGE, has a single N-terminal amino acid sequence. Most of the Thr residues present at the beginning of this sequence are modified; the nature of this modification is still unknown, but O-glycosylation and phosphorylation seem both to be absent. The only potential site for N-glycosylation (Asn 254) is glycosylated in vivo. Most of the eight Cys residues are involved in disulfide bridges. The results are consistent with cruzipain being made of two well-defined domains, a catalytic one with high homology to cathepsin L, and a C-terminal domain, linked to the former by a 'hinge' corresponding to the Pro- and Thr-rich region at its N-terminus.

引用

页码：411 / 416

页数：6