A soluble chloroplast protease processes the Euglena polyprotein precursor to the light harvesting chlorophyll a/b binding protein of photosystem II

被引：14

作者：

Enomoto, T ^{[1
]}

Sulli, C ^{[1
]}

Schwartzbach, SD ^{[1
]}

机构：

[1] UNIV NEBRASKA,SCH BIOL SCI,LINCOLN,NE 68588

来源：

PLANT AND CELL PHYSIOLOGY | 1997年 / 38卷 / 06期

基金：

美国国家科学基金会;

关键词：

chloroplast; Euglena; LHCPII; polyprotein processing; protease;

D O I：

10.1093/oxfordjournals.pcp.a029229

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

The Euglena light harvesting chlorophyll a/b binding protein of photosystem II (LHCPII) is synthesized as a polyprotein precursors composed of 8 LHCPIIs covalently joined by a decapeptide. A soluble chloroplast protease releases LHCPII from the polyprotein. The polyprotein processing peptidase has a pH optima between 8.0 and 9.0. It is inhibited by Zn2+, Cu2+, phenylmethylsulfonyl fluoride and E64 suggesting it is a novel thiol protease.

引用

页码：743 / 746

页数：4

共 20 条

[1]

GIBBS SP, 1993, ORIGINS OF PLASTIDS, P107

[2] THE LIGHT-HARVESTING CHLOROPHYLL A-C-BINDING PROTEIN OF DINOFLAGELLATES - A PUTATIVE POLYPROTEIN [J].