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首页> 外文期刊>Journal of Experimental Botany >Regulation of Rubisco activase and its interaction with Rubisco
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Regulation of Rubisco activase and its interaction with Rubisco

机译：Rubisco活化酶的调控及其与Rubisco的相互作用

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摘要

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.
机译：Rubisco活化酶的大的α-同工型赋予ATP水解的ATP / ADP响应的氧化还原调节和多聚活化酶全酶复合物的Rubisco活化活性。 α-同工型具有包含氧化还原敏感的半胱氨酸残基的C端延伸，其特征是酸性残基含量高。审查了交联和定点诱变研究的C端扩展，提供了氧化还原调节机制的新见解。还审查了有关活化酶和Rubisco之间相互作用的新细节，以及由AAA + 蛋白通常用于底物识别的活化酶“传感器2”域诱变引起的“活化”的可能机制。在该结构域中鉴定了两个活化酶残基，它们与Rubisco识别有关。该结果直接补充了早期研究，后者确定了Rubisco大亚基中活化酶识别的关键残基。

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