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

The Euglena light harvesting chlorophyll a/b binding protein of photosystem II (LHCPII) is synthesized as a polyprotein precursor composed of 8 LHCPIIs covalently joined by a decapeptide. A soluble chloroplast protease releases LHCPII from the polyprotein. The polyprotein processing peptidase has a...

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Veröffentlicht in:Plant and cell physiology 1997, Vol.38 (6), p.743-746
Hauptverfasser: Enomoto, T, Sulli, C, Schwartzbach, S.D
Format: Artikel
Sprache:eng
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Zusammenfassung:The Euglena light harvesting chlorophyll a/b binding protein of photosystem II (LHCPII) is synthesized as a polyprotein precursor 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.
ISSN:0032-0781
1471-9053
DOI:10.1093/oxfordjournals.pcp.a029229