Possible role of the highly conserved amino acids Trp-8 and Pro-13 in the N-terminal segment of the pigment-binding polypeptide LHI alpha of Rhodobacter capsulatus.
Trp-8 and Pro-13 of the Rhodobacter capsulatus light-harvesting (LH) I alpha polypeptide are highly conserved among LHI and LHII alpha 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 alpha polypeptide into the intracytoplasmic membrane (ICM). Pro-13, however, seems not to participate in the integration process of the LHI alpha protein but seems to be important for stable insertion of the LHI beta partner protein in the ICM.
Richter
P
P
Institut für Biologie II, Mikrobiologie, Albert-Ludwigs-Universität, Freiburg, Germany.
Cortez
N
N
Drews
G
G
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D002462:Cell Membrane / Q000378:metabolism; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011392:Proline / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000378:metabolism; D016354:Rhodobacter capsulatus / Q000378:metabolism*; D013057:Spectrum Analysis; D014364:Tryptophan / Q000378:metabolism*
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D021382:Protein Sorting Signals; C094744:light-harvesting complex 1, Rhodospirillum; D014364:Tryptophan; D011392:Proline