caa a22 4500 397557604 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021284 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021284 Truncation of Vargula Luciferase Still Results in Retention of Luminescence [Elektronische Daten] [Yumi Maeda, Hiroshi Ueda, Jim Kazami, Genji Kawano, Eiji Suzuki, Teruyuki Nagamune] 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. © by the Journal of Biochemistry Rapid Communication nationallicence bioluminescence nationallicence luciferase nationallicence protein A nationallicence truncated nationallicence Vargula hilgendorfii nationallicence Maeda Yumi Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut Ueda Hiroshi Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut Kazami Jim Toray Medical Devices & Diagnostics Research Laboratory 3-3-3 Sonoyama, Ohtsu, Shiga 520 aut Kawano Genji Toray Medical Devices & Diagnostics Research Laboratory 3-3-3 Sonoyama, Ohtsu, Shiga 520 aut Suzuki Eiji Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut Nagamune Teruyuki Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 601-603 0021-924X 119:4<601 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021284 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021284 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Maeda Yumi Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Ueda Hiroshi Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kazami Jim Toray Medical Devices & Diagnostics Research Laboratory 3-3-3 Sonoyama, Ohtsu, Shiga 520 aut NATIONALLICENCE 700 1- Kawano Genji Toray Medical Devices & Diagnostics Research Laboratory 3-3-3 Sonoyama, Ohtsu, Shiga 520 aut NATIONALLICENCE 700 1- Suzuki Eiji Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Nagamune Teruyuki Department of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 601-603 0021-924X 119:4<601 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford