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N‐terminal methylation of the core light‐harvesting complex in purple photosynthetic bacteria
Author(s) -
Wang Zheng-Yu,
Shimonaga Masahiro,
Kobayashi Masayuki,
Nozawa Tsunenori
Publication year - 2002
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/s0014-5793(02)02744-8
Subject(s) - rhodobacter , rhodospirillum rubrum , rhodobacter sphaeroides , chromatium , chemistry , purple bacteria , biochemistry , photosynthesis , mass spectrometry , bacteria , amino acid , photosynthetic reaction centre , biology , enzyme , chromatography , gene , genetics , mutant
Several core light‐harvesting complexes from both sulfur and non‐sulfur purple photosynthetic bacteria have been identified to be methylated at the N‐terminal α‐amino group of β‐polypeptides by using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry and nuclear magnetic resonance. Monomethylation has been confirmed for the N‐terminal alanine residues of the β‐polypeptides from Rhodospirillum rubrum , Thermochromatium tepidum and Chromatium vinosum , but not for the β‐polypeptide from Rhodobacter sphaeroides . The modification appears to be related with the amino acid sequence and charge distribution in the N‐terminal end. Some common features and possible functions are discussed.