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The phosphorylation state of chloroplast transit peptides regulates preprotein import.

机译:叶绿体转运肽的磷酸化状态调节前蛋白的导入。

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摘要

Import of nuclear encoded proteins into chloroplast is an essential and well regulated mechanism. The cytosolic kinases STY8, STY17 and STY46 have been shown to phosphorylate chloroplast preprotein transit peptides advantaging the binding of a 14-3-3 dimer. Analyses of sty8 sty17 sty46 mutant plants revealed a role for the kinases in chloroplast differentiation, possibly due to lack of transit peptide phosphorylation. Moreover we could show that not only phosphorylation but also transit peptide dephosphorylation appears to be required for the fine regulation of the back-transport of nuclear encoded proteins to the chloroplast.
机译:将核编码蛋白导入叶绿体是一种必要且受到良好调节的机制。已显示胞质激酶STY8,STY17和STY46磷酸化叶绿体前蛋白转运肽,从而有利于结合14-3-3二聚体。对 sty8 sty17 sty46 突变植物的分析表明,激酶在叶绿体分化中起作用,可能是由于缺乏转运肽磷酸化所致。此外,我们可以证明,不仅需要磷酸化,而且转运肽的去磷酸化似乎对于精细调节核编码蛋白向叶绿体的反向转运是必需的。

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