Open AccessThe Low CO2-Inducible 36-Kilodalton Protein Is Localized to the Chloroplast Envelope of Chlamydomonas reinhardtii
Author(s) -
Ziyadin Ramazanov,
Catherine B. 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.