A Soluble Chloroplast Protease Processes the Euglena Polyprotein Precursor to the Light Harvesting Chlorophyll a/b Binding Protein of Photosystem II

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概要

• 論文の詳細を見る

• 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 Zn^<2+>, Cu^<2+>, phenylmethylsulfonyl fluoride and E64 suggesting it is a novel thiol protease.

• 日本植物生理学会の論文

著者

• Schwartzbach Steven

  School of Biological Sciences, University of Nebraska

• Schwartzbach Steven

  School Of Biological Sciences University Of Nebraska

• Enomoto Toshiki

  School Of Biological Sciences University Of Nebraska:(present)department Of Food Sciences Ishikawa A

• Sulli Chidananda

  School of Biological Sciences, University of Nebraska

• Sulli Chidananda

  School Of Biological Sciences University Of Nebraska

関連論文

• Preferential Loss of Chloroplast Proteins in Nitrogen Deficient Euglena
• Environmental Control of Carbohydrate and Lipid Synthesis in Euglena
• A Soluble Chloroplast Protease Processes the Euglena Polyprotein Precursor to the Light Harvesting Chlorophyll a/b Binding Protein of Photosystem II
• Immunocytochemical Localization of RuBisCO in the Compartmentalized Osmiophilic Body in Dark-Grown Cells of Euglena gracilis Z^1

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