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JXB Advance Access originally published online on March 18, 2008
Journal of Experimental Botany 2008 59(7):1923-1933; doi:10.1093/jxb/erm343
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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

RESEARCH PAPER

Association of Rubisco activase with chaperonin-60β: a possible mechanism for protecting photosynthesis during heat stress

Michael E. Salvucci*

USDA-ARS, Arid-Land Agricultural Research Center, Maricopa, AZ 85238, USA

* To whom correspondence should be addressed. E-mail: mike.salvucci{at}ars.usda.gov

Previous studies have shown that inhibition of photosynthesis by moderate heat stress is a consequence of Rubisco deactivation, caused in part by the thermal instability of Rubisco activase. This involvement of Rubisco activase was confirmed in heat stress and recovery experiments using transgenic Arabidopsis plants. Compared with wild-type plants, photosynthesis, the effective quantum yield of photosystem II, and Rubisco activation were less thermotolerant and recovered more slowly in transgenic Arabidopsis plants with reduced levels of Rubisco activase. Immunoblots showed that 65% of the Rubisco activase was recovered in the insoluble fraction after heat stress in leaf extracts of transgenic but not wild-type plants, evidence that deactivation of Rubisco was a consequence of thermal denaturation of Rubisco activase. The transgenic Arabidopsis plants used in this study contained a modified form of Rubisco activase that facilitated affinity purification of Rubisco activase and proteins that potentially interact with Rubisco activase during heat stress. Sequence analysis and immunoblotting identified the β-subunit of chaperonin-60 (cpn60β), the chloroplast GroEL homologue, as a protein that was bound to Rubisco activase from leaf extracts prepared from heat-stressed, but not control plants. Analysis of the proteins by non-denaturing gel electrophoresis showed that cpn60β was associated with Rubisco activase in a high molecular mass complex. Immunoblot analysis established that the apparent association of cpn60β with Rubisco activase was dynamic, increasing with the duration and intensity of the heat stress and decreasing following recovery. Taken together, these data suggest that cpn60β plays a role in acclimating photosynthesis to heat stress, possibly by protecting Rubisco activase from thermal denaturation.

Key words: Carbon metabolism, heat shock, molecular chaperone, photosynthesis, Rubisco, temperature stress

Received 24 September 2007; Revised 14 November 2007 Accepted 12 December 2007


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