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首页> 外文期刊>Journal of Experimental Botany >Association of Rubisco activase with chaperonin-60β: a possible mechanism for protecting photosynthesis during heat stress
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Association of Rubisco activase with chaperonin-60β: a possible mechanism for protecting photosynthesis during heat stress

机译：Rubisco活化酶与伴侣蛋白60β的关联：在热胁迫期间保护光合作用的可能机制

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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.
机译：先前的研究表明，适度的热胁迫抑制光合作用是Rubisco失活的结果，其部分原因是Rubisco活化酶的热不稳定性。使用转基因拟南芥植物的热胁迫和恢复实验中证实了Rubisco活化酶的这种参与。与野生型植物相比，在具有降低的Rubisco活化酶水平的转基因拟南芥植物中，光合作用，光系统II的有效量子产率和Rubisco活化的耐热性较低，恢复速度较慢。免疫印迹显示，在转基因植物而非野生型植物的叶提取物中进行热胁迫后，不溶级分中回收了65％的Rubisco活化酶，这表明Rubisco失活是Rubisco活化酶热变性的结果。在这项研究中使用的转基因拟南芥植物包含改良形式的Rubisco活化酶，可促进Rubisco活化酶的亲和纯化以及在热胁迫期间可能与Rubisco活化酶相互作用的蛋白质。序列分析和免疫印迹法鉴定了伴侣蛋白60（cpn60β）的β亚基（叶绿体GroEL同源物）是一种与从热胁迫而不是对照植物制备的叶片提取物中的Rubisco激活酶结合的蛋白质。通过非变性凝胶电泳对蛋白质进行的分析表明，cpn60β与高分子量复合物中的Rubisco活化酶有关。免疫印迹分析表明，cpn60β与Rubisco激活酶之间的表观联系是动态的，随着热应激的持续时间和强度的增加而增加，而在恢复后则减少。综上所述，这些数据表明，cpn60β可能通过保护Rubisco激活酶免于热变性而使光合作用适应热胁迫。

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    《Journal of Experimental Botany》 |2008年第7期|p.1923-1933|共11页
  • 作者

    Michael E. Salvucci*;

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

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