Multiple phosphorylation sites in the β subunit of thylakoid ATP synthase
Multiple phosphorylation sites in the β subunit of thylakoid ATP synthase
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DOI：
10.1007/s11120-006-9078-4
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发表时间：
2006-07-01
影响因子：
3.7
通讯作者：
Sabater, Bartolom
中科院分区：
文献类型：
--
作者：
del Riego, Guillermo;Casano, Leonardo M.;Sabater, Bartolom
对大麦（Hordeum vulgare L.）质体ATP合成酶β亚基的蛋白质组学分析表明，成熟蛋白没有羧基末端加工，并通过DNA测序证实了数据库中274个密码子（GAT到AAT）的更正。通过双向电泳（2-DE）分析了ATP合成酶β亚基的6个同工型，pI值在4.95 ~ 5.14之间。质谱分析表明，这六种同工异构体的磷酸化程度不同，与蛋白磷酸酶钙调磷酸酶孵育后，更多的酸性形式消失，证实了这一点。检测到6个Set和/或Thr被磷酸化，其中保守的Thr-179在人线粒体的β亚基中也被磷酸化。这些结果与提出的ATP合酶的磷酸化和14-3-3蛋白调控有关。
Proteomic analyses of the beta subunit of the plastid ATP synthase of barley (Hordeum vulgare L.) revealed that mature protein was not carboxy terminus processed and suggested the correction of the 274 codon (GAT to AAT) in the data bank that was confirmed by DNA sequencing. Six isoforms of the ATP synthase beta subunit with pI ranging from 4.95 to 5.14 were resolved by two-dimensional electrophoresis (2-DE). Mass spectrometry analyses indicated that the six isoforms differ in their phosphorylation degree, which was confirmed by the disappearance of more acidic forms after incubation with the protein phosphatase calcineurin. Six Set and/or Thr were detected as phosphorylated, among them the conserved Thr-179 that is also phosphorylated in the beta subunit of human mitochondria. The results are discussed in relation with the proposed regulation of the ATP synthase by phosphorylation and 14-3-3 proteins.