JXB Advance Access first published online on April 9, 2008
This version published online on April 16, 2008
Journal of Experimental Botany, doi:10.1093/jxb/ern104
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SPECIAL ISSUE REVIEW PAPER |
RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO
1Nara Institute of Science and Technology (NAIST), Graduate School of Biological Sciences, 8916-5 Takayama, Ikoma, Nara, 630-0101 Japan
2Unité des Cyanobactéries, CNRS URA 2172, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France
3Unité de Génétique in silico, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France
4Genetics of Bacterial Genomics, CNRS URA 2171, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France
* To whom correspondence should be addressed. E-mail: ashida{at}bs.naist.jp
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.
Key words: Bacillus subtilis, CO2 fixation, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, methionine salvage pathway, molecular evolution, photosynthesis, RuBisCO, RuBisCO-like protein
Received 30 January 2008; Revised 26 February 2008 Accepted 28 February 2008
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