Cloning, expression and sequence analysis of cDNA for the Ca2+‐binding photoprotein, mitrocomin

FEBS Letters

Fagan, Thomas F.³  Tsuji, Frederick I.³  Blinks, John R.²  Inouye, Satoshi¹  Ohmiya, Yoshihiro³ 

[1] Marine Biology Research Division 0202, Scripps Institution of Oceanography, University of California at San Diego, La Jolla, CA 92093. USA;Friday Harbor Laboratories, University of Washington, Friday Harbor, WA 98250, USA;Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565, Japan

关键词: Bioluminescence;    Halistaura;    Calcium;    Aequorin;    Clytin;    C-terminal tyrosine;   

DOI  :  10.1016/0014-5793(93)80675-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The primary structure of mitrocomin consists of 190 amino acid residues, with three Ca²⁺-binding sites and a tyrosine residue at the C-terminus. Mitrocomin shows an amino acid sequence homology of 67.9% and 60.7% when compared with aequorin and clytin, respectively. The amino acid residues Cys¹⁵², His⁵⁸, His¹⁶⁹, Trp¹², Trp⁸⁶, Trp¹⁰⁸, Trp¹²⁹ and Trp¹⁷³ are conserved in all three photoproteins, suggesting that they play a role in light emission.

【 授权许可】

Unknown