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γ‐ N ‐Methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix
Author(s) -
Rümbeli Robert,
Suter Franz,
Wirth Monica,
Sidler Walter,
Zuber Herbert
Publication year - 1987
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(87)80341-1
Subject(s) - phycobiliprotein , cyanobacteria , allophycocyanin , asparagine , residue (chemistry) , chemistry , biochemistry , amino acid , stereochemistry , biology , phycocyanin , bacteria , genetics
Reinvestigation of the amino acid sequences of all phycobiliproteins from Mastigocladus laminosus showed that there is a post‐translationally modified asparagine residue at position 72 of the phycobiliprotein subunits β PC , β AP and β 16.2 . This residue was identified as γ‐ N ‐methylasparagine and it was also found in β PE of Calothrix . This study also revealed some differences in the amino acid sequences β AP and β PC compared to the published data.