N‐terminal sequence analysis of the 8 kDa protein in Chlamydomonas reinhardii Localization of the phosphothreonine

FEBS Letters

Dedner, Norbert³  Meyer, Helmut E.²  Wildner, Günter F.³  Ashton, Chris¹ 

[1] Applied Biosystems, D-6108 Weiterstadt, FRG;Institut für Physiologische Chemie, Ruhr-Universität Bochum, Postfach 102148, D-4630 Bochum 1, FRG;Lehrstuhl Biochemie der Pflanzen, Ruhr-Universität Bochum, Postfach 102148, D-4630 Bochum 1, FRG

关键词: Photosystem II;    psb H protein;    N-terminal sequence;    Phosphothreonine;    (Chlamydomonas reinhardii);    DTT;    dithiothreitol;    LHC-II;    polypeptides of the light-harvesting chlorophyll a/b protein complex;    Mops;    3-(N-morpholino)propanesulfonic acid;    OEC;    oxygen evolving complex;    PTC;    phenylthiocarbamyl;    PTH;    phenylthiohydantoin;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(88)80288-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A phosphorylated 8 kDa protein of Chlamydomonas reinhardii thylakoids has been isolated and its N-terminal amino acid sequence determined by gas-phase sequencing. The sequence analysis of the 48 amino acid residues revealed that this protein is about 50% homologous to the psb H gene products of higher plants. In contrast to them, it contains an insert of seven amino acid residues (Ser-5 to Lys-11). The first threonine residue was phosphorylated as determined by ³²P detection during sequencing and also by analysis of the modified degradation products in the chemical reaction of the Edman degradation process. This latter method allows the identification of phosphorylated threonine residues without radiolabelling the protein.

【 授权许可】

Unknown