Heterologous expression and initial characterization of recombinant RbcX protein from Thermosynechococcus elongatus BP-1 and the role of RbcX in RuBisCO assembly

• Authors: Miroslaw Tarnawski , Beata Gubernator , Piotr Kolesinski , Andrzej Szczepaniak
• Languages of publication: EN

Abstracts

EN

In the cyanobacterial RuBisCO operon from Thermosynechococcus elongatus the rbcX gene is juxtaposed and cotranscribed with the rbcL and rbcS genes which encode large and small RuBisCO subunits, respectively. It has been suggested that the rbcX position is not random and that the RbcX protein could be a chaperone for RuBisCO. In this study, the RbcX protein from T. elongatus was overexpressed, purified and preliminary functional studies were conducted. The recombinant protein purified from Escherichia coli extracts was predominantly present in a soluble fraction in a dimeric form. Coexpression experiments have demonstrated that RbcX can mediate RbcL dimer (L2) formation, and that it is essential for the L8 core complex assembly. This is the first characterization of the RbcX protein from a thermophilic organism.

Keywords

EN

RbcX; purification; expression; Thermosynechococcus elongatus; RuBisCO assembly

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2008
• Volume: 55
• Issue: 4
• Pages: 777-785

Dates

published

2008

received

2008-06-18

revised

2008-10-22

accepted

2008-12-03

(unknown)

2008-12-16

Contributors

author

Miroslaw Tarnawski

• Department of Biophysics, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland

author

Beata Gubernator

• Department of Biophysics, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland

author

Piotr Kolesinski

• Department of Biophysics, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland

author

Andrzej Szczepaniak

• Department of Biophysics, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland

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