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

• Autorzy: Tarnawski M. , Gubernator B. , Kolesinski P. , Szczepaniak A.
• Języki publikacji: EN

Abstrakty

EN

In the cyanobacterial RuBisCO operon from Thermosynechococcus elongatus the rbc X 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.

Słowa kluczowe

PL

rbcX gene; rbcL gene; rbcS gene; RuBisCO assembly; purification; protein expression; Thermosynechococcus elongatus; Escherichia coli; enzyme; photosynthesis; thermophilic organism

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 4
• Strony: 777-785
• Opis fizyczny: p.777-785,fig.,ref.

Twórcy

autor

Tarnawski M.

• University of Wroclaw, Przybyszewskiego 63/77, 51-148 Wroclaw, Poland

autor

Gubernator B.

autor

Kolesinski P.

autor

Szczepaniak A.

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