@article{oai:matsumoto-u.repo.nii.ac.jp:00001369,
 author = {山田, 一哉 and 三島, 歩実 and 花岡, 由紀奈 and 三崎, 紀展 and 上條, 茜 and 坂本, 那津子 and 茅野, 友加里 and 堀内, 涼香 and 近藤, 晴菜 and 長井, 朱里 and 丸山, ゆきの and 山根, 優奈 and 田野口, 愛華 and 塚田, 晃子 and 髙木, 勝広},
 journal = {松本大学研究紀要, The Journal of Matsumoto University},
 month = {Mar},
 note = {application/pdf, The rat enhancer of split- and hairy-related protein-2 (SHARP-2) is a basic helix-loop-helix transcriptional repressor. Many transcription factors interact with other proteins to form complex transcriptional regulation networks. To identify a SHARP-2-interacting protein(s), we screened a rat liver cDNA library using a yeast two-hybrid system. Approximately 3.5×107  independent clones were screened and 29 positive clones were obtained. Of these, multiple clones contained AT motif-binding factor-1 (ATBF1) and Sex-determining region Y-box 6 (Sox6) which both were transcription factors. We then focused on and analyzed physical protein-protein interaction of SHARP-2 with ATBF1 and Sox6. First, minimal interaction domain of ATBF1 and Sox6 with the SHARP-2 was determined. Amino acid residues between 3,271 and 3,379 of the ATBF1 and those between 201 and 362 of Sox6 were required for an interaction with SHARP-2, respectively. We then examined which domain of SHARP-2 is required for interactions with ATBF1 and Sox6. Amino acid residues between 301 and 355 of the SHARP-2 interacted with the ATBF1 and those between 384 and 397 of the SHARP-2 interacted with the Sox6. Thus, we concluded that both the ATBF1 and Sox6 were identified as the SHARP-2-interacting protein and that the SHARP-2 interacted with them using different domains.},
 pages = {105--115},
 title = {SHARP-2相互作用タンパク質の同定と特性},
 volume = {20},
 year = {2022}
}