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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/50470

Title: The dimerization domain upstream binding factor contains multiple helical structures
Authors: Lai YS
Tseng HB
Hu CH
Contributors: 國立臺灣海洋大學:生命科學暨生物科技學系
Date: 1996-03
Issue Date: 2018-10-09T02:59:43Z
Publisher: Biochem Biophys Res Commun.
Abstract: Abstract: The upstream binding factor, UBF, is an RNA polymerase I transcription factor which contains multiple DNA binding domains and a novel protein dimerization domain. Active UBF forms homodimers in vivo through the intramolecular interactions of its dimerization domain, which spans a hundred amino-terminal residues. In the presence of both UBF dimerization domain and its immediately adjacent lysine-rich basic DNA binding domain, the E. coli expressed recombinant polypeptide, dbUBF (dimerization plus basic motifs of UBF), forms homodimers in vitro and binds to double-stranded DNA nonselectively. In gel retardation assay, dbUBF dimers make multiple shift-ladders corresponding to numerous protein dimer-DNA complexes. The UBF dimerization domain contains multiple helical structures, as predicted by EMBO-PHD program. Most of hydrophobic residues in the dimerization domain are confined in the hydrophobic phase of these hypothetic helices. Mutating these hydrophobic residues to glutamate prohibits dbUBF association and gives a different shift pattern in gel retardation assay. The results we present here argue that UBF association is largely exerted by the hydrophobic interactions between the multiple helices to bring two molecules together.
Relation: 220(3) pp.816-823
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/50470
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

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