Journal Article

Regulation of Rubisco activase and its interaction with Rubisco

Archie R. Portis, Cishan Li, Dafu Wang and Michael E. Salvucci

in Journal of Experimental Botany

Published on behalf of Society for Experimental Biology

Volume 59, issue 7, pages 1597-1604
Published in print May 2008 | ISSN: 0022-0957
Published online November 2007 | e-ISSN: 1460-2431 | DOI: http://dx.doi.org/10.1093/jxb/erm240
Regulation of Rubisco activase and its interaction with Rubisco

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The large, α-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 α-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.

Keywords: AAA+ protein; cross-linking; redox regulation; Rubisco

Journal Article.  4067 words.  Illustrated.

Subjects: Plant Sciences and Forestry

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