共查询到20条相似文献,搜索用时 15 毫秒
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Gastrin gene expression and regulation in rat islet cell lines 总被引:1,自引:0,他引:1
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Transcriptional regulation of the CLC-K1 promoter by myc-associated zinc finger protein and kidney-enriched Krüppel-like factor, a novel zinc finger repressor
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Uchida S Tanaka Y Ito H Saitoh-Ohara F Inazawa J Yokoyama KK Sasaki S Marumo F 《Molecular and cellular biology》2000,20(19):7319-7331
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A novel, tissue-restricted zinc finger protein (HF-1b) binds to the cardiac regulatory element (HF-1b/MEF-2) in the rat myosin light-chain 2 gene. 总被引:7,自引:4,他引:3
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H Zhu V T Nguyen A B Brown A Pourhosseini A V Garcia M van Bilsen K R Chien 《Molecular and cellular biology》1993,13(7):4432-4444
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Fahu He Weirong Dang Chikage Abe Kengo Tsuda Makoto Inoue Satoru Watanabe Naohiro Kobayashi Takanori Kigawa Takayoshi Matsuda Takashi Yabuki Masaaki Aoki Eiko Seki Takushi Harada Yuri Tomabechi Takaho Terada Mikako Shirouzu Akiko Tanaka Peter Güntert Yutaka Muto Shigeyuki Yokoyama 《Protein science : a publication of the Protein Society》2009,18(1):80-91
The muscleblind‐like (MBNL) proteins 1, 2, and 3, which contain four CCCH zinc finger motifs (ZF1–4), are involved in the differentiation of muscle inclusion by controlling the splicing patterns of several pre‐mRNAs. Especially, MBNL1 plays a crucial role in myotonic dystrophy. The CCCH zinc finger is a sequence motif found in many RNA binding proteins and is suggested to play an important role in the recognition of RNA molecules. Here, we solved the solution structures of both tandem zinc finger (TZF) motifs, TZF12 (comprising ZF1 and ZF2) and TZF34 (ZF3 and ZF4), in MBNL2 from Homo sapiens. In TZF12 of MBNL2, ZF1 and ZF2 adopt a similar fold, as reported previously for the CCCH‐type zinc fingers in the TIS11d protein. The linker between ZF1 and ZF2 in MBNL2 forms an antiparallel β‐sheet with the N‐terminal extension of ZF1. Furthermore, ZF1 and ZF2 in MBNL2 interact with each other through hydrophobic interactions. Consequently, TZF12 forms a single, compact global fold, where ZF1 and ZF2 are approximately symmetrical about the C2 axis. The structure of the second tandem zinc finger (TZF34) in MBNL2 is similar to that of TZF12. This novel three‐dimensional structure of the TZF domains in MBNL2 provides a basis for functional studies of the CCCH‐type zinc finger motifs in the MBNL protein family. 相似文献
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Rui Wang Jingman Ni Xiaoyu Hu Yaping Ma Xiangqun Li Dingjian Yang Shouliang Dong Xiaowu Yang Xinfu Pan 《中国科学C辑(英文版)》1997,40(5):518-523
The second zinc finger fragment of Sp1 (Sp1-ZF2), its mutant (Sp1-ZF2/HT. E20 → H, R23 → T), and two mimic analogues (ZF20 and ZF15) were synthesized by stepwise solid phase technique. The CD spectra and UV-visible spectrum with CoC12 indicated that the formation of zinc finger structure was affected not only by the hydrophobic amino acids but also by the change of the distance between Cys and His. Gel-retardat ion electrophoresis assays indicated that the Glu and Arg residues are very important for recognition. A single zinc finger like Sp1-ZF2 is able to bind DNA sequence specifically. 相似文献