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JXB Advance Access published online on February 16, 2008
Journal of Experimental Botany, doi:10.1093/jxb/erm361
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© 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

Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships

F. Robert Tabita1,2,3,*, Sriram Satagopan2, Thomas E. Hanson4, Nathan E. Kreel3 and Stephanie S. Scott2

1Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA
2The Plant Molecular Biology Biology/Biotechnology Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA
3The OSU Biochemistry Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA
4College of Marine and Earth Studies, Delaware Biotechnology Institute, University of Delaware, 127 DBI, 15 Innovation Way, Newark, DE 19711, USA

* To whom correspondence should be addressed at the Department of Microbiology, The Ohio State University. E-mail: Tabita.1{at}osu.edu

There are four forms of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) found in nature. Forms I, II, and III catalyse the carboxylation and oxygenation of ribulose 1,5-bisphosphate, while form IV, also called the Rubisco-like protein (RLP), does not catalyse either of these reactions. There appear to be six different clades of RLP. Although related to bona fide Rubisco proteins at the primary sequence and tertiary structure levels, RLP from two of these clades is known to perform other functions in the cell. Forms I, II, and III Rubisco, along with form IV (RLP), are thought to have evolved from a primordial archaeal Rubisco. Structure/function studies with both archaeal form III (methanogen) and form I (cyanobacterial) Rubisco have identified residues that appear to be specifically involved with interactions with molecular oxygen. A specific region of all form I, II, and III Rubisco was identified as being important for these interactions.

Key words: CBB cycle, different forms, evolution, Rubisco, structure/function

Received 22 October 2007; Revised 29 November 2007 Accepted 18 December 2007


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