A Soluble Chloroplast Protease Processes the Euglena Polyprotein Precursor to the Light Harvesting Chlorophyll a/b Binding Protein of Photosystem II
Abstract
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.
Publication Title
Plant and Cell Physiology
Recommended Citation
Enomoto, T., Sulli, C., & Schwartzbach, S. (1997). 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), 743-746. https://doi.org/10.1093/oxfordjournals.pcp.a029229
