Truncation of Vargula luciferase still results in retention of luminescence.
Significant amino acid sequence homology in two regions of Vargula hilgendorfii to one in apoaequorin was reported. The intra-amino acid homology in Vargula luciferase between residues 81-312 and 321-540 was 19.3%, and each of this intra-homologous region contained the region homologous to apoaequorin. In order to prove the possibility that only one of the homologous regions is sufficient for luminescence, we have produced a chimeric protein comprising of only the N-terminal homologous region of Vargula luciferase fused to protein A. Comparison of the luminescence of this truncate luciferase indicated that there was 38.5% retention in the bioluminescence of luciferase when compared to that of the mature form of luciferase. This fact may have interesting implications for further study of engineering luciferase.
Maeda
Y
Y
Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo.
Ueda
H
H
Kazami
J
J
Kawano
G
G
Suzuki
E
E
Nagamune
T
T
D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002522:Chlorocebus aethiops; D003445:Crustacea / Q000201:enzymology* / Q000235:genetics; D005796:Genes / Q000235:genetics; D008156:Luciferases / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D008163:Luminescent Measurements; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D017384:Sequence Deletion / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D013205:Staphylococcal Protein A / Q000235:genetics
D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D008156:Luciferases