Skip Navigation


JXB Advance Access originally published online on April 9, 2008
Journal of Experimental Botany 2008 59(7):1543-1554; doi:10.1093/jxb/ern104
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
59/7/1543    most recent
ern104v2
ern104v1
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Ashida, H.
Right arrow Articles by Yokota, A.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ashida, H.
Right arrow Articles by Yokota, A.
Agricola
Right arrow Articles by Ashida, H.
Right arrow Articles by Yokota, A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author [2008]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

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

Hiroki Ashida1,*, Yohtaro Saito1, Toshihiro Nakano1, Nicole Tandeau de Marsac2, Agnieszka Sekowska3, Antoine Danchin4 and Akiho Yokota1

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.