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J. Biochem, 1996, Vol. 119, No. 4 601-603
© 1996 Japanese Biochemical Society

research-article

Truncation of Vargula Luciferase Still Results in Retention of Luminescence

Yumi Maeda*,1, Hiroshi Ueda*, Jim Kazami{dagger}, Genji Kawano{dagger}, Eiji Suzuki* and Teruyuki Nagamune*

*Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113
{dagger}Toray Medical Devices & Diagnostics Research Laboratory 3-3-3 Sonoyama, Ohtsu, Shiga 520

1 To whom correspondence should be addressed. E-mail: yumi{at}bio.t.u-tokyo.ac.jp

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 truncated 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 engineered luciferase.


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