A SOLUBLE CHLOROPLAST PROTEASE PROCESSES THE EUGLENA POLYPROTEIN PRECURSOR TO THE LIGHT-HARVESTING CHLOROPHYLL A B BINDING-PROTEIN OF PHOTOSYSTEM-II/

Authors
ENOMOTO T SULLI C SCHWARTZBACH SD
Citation
T. Enomoto et al., A SOLUBLE CHLOROPLAST PROTEASE PROCESSES THE EUGLENA POLYPROTEIN PRECURSOR TO THE LIGHT-HARVESTING CHLOROPHYLL A B BINDING-PROTEIN OF PHOTOSYSTEM-II/, Plant and Cell Physiology, 38(6), 1997, pp. 743-746
Citations number
20
Categorie Soggetti
Plant Sciences
Journal title
Plant and Cell Physiology → ACNP
ISSN journal
00320781
Volume
38
Issue
6
Year of publication
1997
Pages
743 - 746
Database
ISI
SICI code
0032-0781(1997)38:6<743:ASCPPT>2.0.ZU;2-Z
Abstract
The Euglena light harvesting chlorophyll a/b binding protein of photos ystem 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 proces sing 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.