caa a22 4500 397555717 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021547 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021547 Purification, Characterization, and cDNA Cloning of ABP-2 (Aryiphorin Gene-Specific Binding Protein-2) That Specifically Binds to the ABP-1-Binding Sequence in the Arylphorin Gene of Sarcophaga peregrina [Elektronische Daten] [Nobuaki Adachi, Takeo Kubo, Shunji Natori] Previously, we demonstrated that ABP-1 (aryiphorm gene-specific binding protein-1), which is suggested to be the transcriptional activator of the aryiphorin gene of Sarcophaga peregrina, is present in NIH-Sape-4 cells, which do not express aryiphorin. As well as ABP-1, these cells were found to contain another protein (ABP-2) that probably binds to the same sequence as that to which ABP-1 binds [ Adachi, N., Kubo, T., and Natori, S. (1993) J. Biochem. 114, 55-60]. We purified ABP-2 from a nuclear extract of NIH-Sape-4 cells and compared its DNA-binding activity with that of ABP-1. Both ABP-1 and ABP-2 were found to bind to the same sequence in the arylphorin gene with the same affinity and stability, but an ABP-2-specific hypersensitive site was detected by DNase I footprinting analysis. Analyses of proteolytic fragments suggested that both ABP-1 and ABP-2 have Zn fingers showing high similarity with that of AEF-1, a transcriptional repressor of the Drosophila melanogaster alcohol dehydrogenase gene that binds to a sequence very similar to that binding ABP-1 and ABP-2. We isolated a candidate cDNA for ABP-2, and the protein encoded contained nine Zn fingers and regions rich in alanine, glutamine, serine/threonine, glycine, histidine, and asparagine. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence ABP-1 nationallicence ABP-2 nationallicence arylphorin gene nationallicence Sarcophaga peregrina nationallicence transcription factor nationallicence Adachi Nobuaki Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut Kubo Takeo Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut Natori Shunji Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1239-1246 0021-924X 120:6<1239 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021547 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021547 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Adachi Nobuaki Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kubo Takeo Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Natori Shunji Faculty of Parmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1239-1246 0021-924X 120:6<1239 1996 120 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