Dilly-Hartwig H, Allen J F, Paulsen H, Race H L
Institut für Allgemeine Botanik, Johannes Gutenberg-Universität Mainz, Germany.
FEBS Lett. 1998 Sep 11;435(1):101-4. doi: 10.1016/s0014-5793(98)01046-1.
Previous studies directed towards understanding phosphorylation of the chlorophyll alb binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhch1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of which are discussed.
以往致力于理解构成光捕获复合体II（LHC II）的叶绿素a/b结合蛋白磷酸化的研究，都集中在成熟蛋白靠近N端的单个磷酸化位点上。在此我们表明，一系列重组豌豆Lhcb1蛋白，每个都缺失包括该位点在内的N端片段，但仍被与光系统II核心复合体制剂相关的蛋白激酶磷酸化。然而，缺失前58个氨基酸残基的Lhch1蛋白未被磷酸化。结果表明，LHC II蛋白在一个或多个位点被磷酸化，对此我们将讨论其意义。
