Posttranslational modifications of the beta subunit of a cryptomonad phycoerythrin. Sites of bilin attachment and asparagine methylation.

@article{Wilbanks1989PosttranslationalMO,
  title={Posttranslational modifications of the beta subunit of a cryptomonad phycoerythrin. Sites of bilin attachment and asparagine methylation.},
  author={Sigurd M. Wilbanks and Gary J. Wedemayer and Alexander N. Glazer},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 30},
  pages={17860-7}
}
Determination of the partial amino acid sequence of the beta subunit of cryptomonad strain CBD phycoerythrin 566 established the nature, locations, and modes of attachment of the three bilin prosthetic groups and revealed a site of posttranslational methylation. Isolation of peptides cross-linked by a phycobiliviolin led to an unambiguous assignment of two thioether linkages, from residues beta-Cys-50 and beta-Cys-61 to this bilin. Two bilins were attached through single thioether linkages, a… CONTINUE READING