γ‐N‐Methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix

FEBS Letters

Zuber, Herbert¹  Wirth, Monica¹  Rümbeli, Robert¹  Suter, Franz¹  Sidler, Walter¹ 

[1] Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland

关键词: γ-N-Methylasparagine;    Posttranslational modification;    Phycobiliprotein;    Amino acid sequence;    (Mastigocladus laminosus;    Calothrix);    AP;    allophycocyanin;    PC;    C-phycocyanin;    PEC;    phycoerythrocyanin;    PE;    C-phycoerythrin;    α and β;    subunits of phycobiliproteins;    L8.9 C;    linker polypeptide of the AP core;   

DOI  :  10.1016/0014-5793(87)80341-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown