Institut für Allgemeine Botanik, Johannes Gutenberg-Universität, 55099, Mainz, Germany.
Photosynth Res. 1994 Jun;40(3):269-77. doi: 10.1007/BF00034776.
The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.
确定了 Mantoniella squamata 叶绿素 a/b/c 结合蛋白的一级结构。这是首次报道蛋白质测序揭示了一个修饰氨基酸,导致 LHCP 特异性 TFA 切割位点。将 Mantoniella 的序列与其他叶绿素 a/b-和叶绿素 a/c-结合蛋白进行比较表明,修饰氨基酸位于这些蛋白质高度保守的区域。比对还表明,Mantoniella 的 LHCP 与叶绿素 a/b 结合蛋白有关。最后,讨论了可能的叶绿素结合区域。