PHOSPHORYLATION OF CHLOROPLAST MEMBRANE POLYPEPTIDES
PHOSPHORYLATION OF CHLOROPLAST MEMBRANE POLYPEPTIDES
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DOI：
10.1038/269344a0
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发表时间：
1977-01-01
期刊：
影响因子：
64.8
通讯作者：
BENNETT, J
中科院分区：
文献类型：
--
作者：
BENNETT, J
叶绿体类囊体的光照导致膜的所谓高能态的形成1 -3。这种状态的建立伴随着膜内的几种结构变化，包括偶联因子4的构象变化，光系统II对化学探针重氮苯磺酸盐5的可及性增加，以及堆叠类囊体之间的分区厚度减少6。我在这里描述了一个相当不同类型的结构变化，以前没有报道的叶绿体膜蛋白磷酸化。与上述变化一样，蛋白质磷酸化是一种可逆的、能量依赖性的膜修饰，但它与其他变化的不同之处在于它采取了涉及某些可识别的叶绿体膜多肽的特定化学反应的形式。这些多肽中最引人注目的是捕光叶绿素b结合蛋白，最丰富的类囊体多肽7。
ILLUMINATION of chloroplast thylakoids leads to the formation of the so-called high energy state of the membrane1–3. The establishment of this state is accompanied by several structural changes within the membrane, including a conformational change in the coupling factor4, increased accessibility of photosystem II to the chemical probep-diazonium benzene sulphonate5, and a reduction in the thickness of the partition between stacked thylakoids6. I describe here a rather different type of structural change that has not previously been reported for chloroplast membranes—protein phosphorylation. Like the above changes, protein phosphorylation is a reversible, energy-dependent membrane modification, but it differs from the other changes in that it takes the form of a specific chemical reaction involving certain identifiable chloroplast membrane polypeptides. The most conspicuous of these polypeptides is the light-harvesting chlorophylla/bbinding protein, the most abundant thylakoid polypeptide7.