The Low CO2-Inducible 36-Kilodalton Protein Is Localized to the Chloroplast Envelope of Chlamydomonas reinhardtii | Zendy

Zakir Ramazanov | Zendy; Catherine Mason | Zendy; Anne M. Geraghty | Zendy; Martin H. Spalding | Zendy; James V. Moroney | Zendy

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The Low CO2-Inducible 36-Kilodalton Protein Is Localized to the Chloroplast Envelope of Chlamydomonas reinhardtii

Author(s) -

Zakir Ramazanov,

Catherine Mason,

Anne M. Geraghty,

Martin H. Spalding,

James V. Moroney

Publication year - 1993

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.101.4.1195

Subject(s) - chlamydomonas reinhardtii , chloroplast , chloroplast membrane , kilodalton , carbonic anhydrase , membrane , chlamydomonas , biochemistry , biophysics , biology , chemistry , microbiology and biotechnology , thylakoid , enzyme , gene , mutant

The localization of the 36-kD polypeptide of Chlamydomonas reinhardtii induced by photoautotrophic growth on low CO2 concentrations (0.03% in air [v/v], low CO2-grown cells) has been investigated. This polypeptide was specifically localized to the chloroplast envelope membranes isolated from low CO2-grown cells and was not present in the chloroplast envelopes isolated from high (5% CO2 in air [v/v]) CO2-grown cells. The 36-kD protein does not show carbonic anhydrase activity and was not present on the plasma membranes isolated from low CO2-grown cells. This protein may, in part, account for the different inorganic carbon uptake characteristics observed in chloroplasts isolated from high and low CO2-grown cells of C. reinhardtii.

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