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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
Author(s) -
Richter Petra,
Cortez Néstor,
Drews Gerhart
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80729-m
Subject(s) - rhodobacter , terminal (telecommunication) , chemistry , pigment , biochemistry , amino acid , amino acid residue , stereochemistry , peptide sequence , organic chemistry , gene , mutant , telecommunications , computer science
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.