Journal Article

RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO

Hiroki Ashida, Yohtaro Saito, Toshihiro Nakano, Nicole Tandeau de Marsac, Agnieszka Sekowska, Antoine Danchin and Akiho Yokota

in Journal of Experimental Botany

Published on behalf of Society for Experimental Biology

Volume 59, issue 7, pages 1543-1554
Published in print May 2008 | ISSN: 0022-0957
Published online April 2008 | e-ISSN: 1460-2431 | DOI: http://dx.doi.org/10.1093/jxb/ern104
RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the key enzyme in the fixation of CO2 in the Calvin cycle of plants. Many genome projects have revealed that bacteria, including Bacillus subtilis, possess genes for proteins that are similar to the large subunit of RuBisCO. These RuBisCO homologues are called RuBisCO-like proteins (RLPs) because they are not able to catalyse the carboxylase or the oxygenase reactions that are catalysed by photosynthetic RuBisCO. It has been demonstrated that B. subtilis RLP catalyses the 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) enolase reaction in the methionine salvage pathway. The structure of DK-MTP-1-P is very similar to that of ribulose-1,5-bisphosphate (RuBP) and the enolase reaction is a part of the reaction catalysed by photosynthetic RuBisCO. In this review, functional and evolutionary relationships between B. subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO are discussed. In addition, the fundamental question, ‘How has RuBisCO evolved?’ is also considered, and evidence is presented that RuBisCOs evolved from RLPs.

Keywords: Bacillus subtilis; CO2 fixation; 2,3-diketo-5-methylthiopentyl-1-phosphate enolase; methionine salvage pathway; molecular evolution; photosynthesis; RuBisCO; RuBisCO-like protein

Journal Article.  6346 words.  Illustrated.

Subjects: Plant Sciences and Forestry

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