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Plant and Cell Physiology Advance Access originally published online on May 7, 2008
Plant and Cell Physiology 2008 49(6):994-997; doi:10.1093/pcp/pcn074
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Short Communication

Identification and Localization of the CupB Protein Involved in Constitutive CO2 Uptake in the Cyanobacterium, Synechocystis sp. Strain PCC 6803

Min Xu1, Teruo Ogawa1,2, Himadri B. Pakrasi2 and Hualing Mi1,*

1National Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Graduate courses of the Chinese Academy of Sciences, 300 Fenglin Road, Shanghai, 200032, PR China
2Department of Biology, Washington University, St Louis, MO 63130, USA

*Corresponding author: E-mail, mihl{at}sippe.ac.cn; Fax, +86-21-54924015.


  Abstract

Antibody against cMyc cross-reacted strongly with the CupB protein tagged with His6-cMyc (HM) in thylakoid membrane of Synechocystis sp. strain PCC 6803 but only faintly with the cytoplasmic membrane fraction. The protein was not detected in the membranes of the {Delta}ndhD4 and {Delta}ndhF4 mutants in which CupB was tagged with HM. We concluded that a CupB complex containing NdhD4 and NdhF4 is largely, if not exclusively, confined to the thylakoid membrane. Both CupB and NdhH were detected in a fraction containing protein complexes of > 450 kDa, obtained after nickel column and gel filtration chromatography of the membranes solubilized with n-dodecyl-β-maltoside.

Keywords: CO2 uptake - CupB - Cytoplasmic membrane - NDH-1 - Synechocystis 6803 - Thylakoid membrane

Abbreviations: CM, cytoplasmic membrane; HC, high CO2-grown; HM, His6-cMyc; LC, low CO2-adapted; DM, n-dodecyl-β-maltoside; TM, thylakoid membrane; WT, wild type.

(Received February 4, 2008; Accepted May 1, 2008)
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