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

• Published in: FEBS letters Vol. 333; no. 3; pp. 301 - 305
• Main Authors: Fagan, Thomas F., Ohmiya, Yoshihiro, Blinks, John R., Inouye, Satoshi, Tsuji, Frederick I.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 01-11-1993
• Subjects: Aequorin; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Bioluminescence; C-terminal tyrosine; Calcium; Clytin; Fundamental and applied biological sciences. Psychology; Halistaura; Non metallic chromoproteins, photoproteins; Proteins; Tyrosine; Bioluminescence; Calcium; Nucleotide sequence; Primary structure; Binding site; Gene expression; Photoprotein; Proteins; Binding protein; Emission spectrometry; Complementary DNA; Aminoacid; Molecular cloning; Nucleic acid; Aminoacid sequence
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)80675-K

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.