Possible role of the highly conserved amino acids Trp‐8 and Pro‐13 in the N‐terminal segment of the pigment‐binding poly eptide LHI α of Rhodobacter capsulatus

FEBS Letters

Cortez, Néstor¹  Richter, Petra¹  Drews, Gerhart¹ 

[1] Institut für Biologie II, Mikrobiologie, Schänzlestraße 1, Albert-Ludwigs-Universität, W-7800 Freiburg, Germany

关键词: LHI α polypeptide;    Membrane insertion;    Signal peptide;    Site-directed mutagenesis;    Rhodobacter capsulatus;    SDS;    sodium dodecyl sulfate;    LH;    light-harvesting;    RC;    reaction center;    Bchl;    bacteriochlorophyll;    ICM;    intracytoplasmic membrane;    PSU;    photosynthetic unit;   

DOI  :  10.1016/0014-5793(91)80729-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Trp-8 and Pro-13 of the Rhodobacter capsulatus light-harvesting (LH) I α polypeptide are highly conserved among LHI and LHII α proteins of several species of the Rhodospirillaceae. Exchange of Trp-8 and Pro-13 to other amino acyl residues similar in structure and/or hydrophobicity indicates that Trp-8 is involved in the insertion of the LHI α polypeptide into the intracytoplasmic membrane (ICM). Pro-13, however, seems not to participate in the integration process of the LHI α protein but seems to be important for stable insertion of the LHI β partner protein in the ICM.

【 授权许可】

Unknown