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JXB Advance Access originally published online on November 29, 2007
Journal of Experimental Botany 2008 59(7):1597-1604; doi:10.1093/jxb/erm240
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© The Author [2007]. 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

Regulation of Rubisco activase and its interaction with Rubisco

Archie R. Portis, Jr1,2,*, Cishan Li2 {dagger}, Dafu Wang2 and Michael E. Salvucci3

1USDA-ARS, Photosynthesis Research Unit, Urbana, IL 61801, USA
2University of Illinois, Department of Plant Biology, Urbana, IL 61801, USA
3USDA-ARS, Arid-Land Agricultural Research Center, Maricopa, AZ 85239, USA

* To whom correspondence should be addressed. E-mail: arportis{at}uiuc.edu

The large, {alpha}-isoform of Rubisco activase confers redox regulation of the ATP/ADP response of the ATP hydrolysis and Rubisco activation activities of the multimeric activase holoenzyme complex. The {alpha}-isoform has a C-terminal extension that contains the redox-sensitive cysteine residues and is characterized by a high content of acidic residues. Cross-linking and site-directed mutagenesis studies of the C-terminal extension that have provided new insights into the mechanism of redox regulation are reviewed. Also reviewed are new details about the interaction between activase and Rubisco and the likely mechanism of ‘activation’ that resulted from mutagenesis in a ‘Sensor 2’ domain of activase that AAA+ proteins often use for substrate recognition. Two activase residues in this domain were identified that are involved in Rubisco recognition. The results directly complement earlier studies that identified critical residues for activase recognition in the large subunit of Rubisco.

Key words: AAA+ protein, cross-linking, redox regulation, Rubisco

{dagger} Present address: Institute of Human Virology, University of Maryland School of Medicine, 725 West Lombard Street, Baltimore, MD 21201, USA.

Received 31 July 2007; Revised 24 August 2007 Accepted 11 September 2007


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