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Titolo:
Effect of arginine mutation of alanine-556 on DNA recognition of zinc finger protein Sp1
Autore:
Matsushita, K; Sugiura, Y;
Indirizzi:
Kyoto Univ, Inst Chem Res, Uji, Kyoto 6110011, Japan Kyoto Univ Uji KyotoJapan 6110011 st Chem Res, Uji, Kyoto 6110011, Japan
Titolo Testata:
BIOORGANIC & MEDICINAL CHEMISTRY
fascicolo: 9, volume: 9, anno: 2001,
pagine: 2259 - 2267
SICI:
0968-0896(200109)9:9<2259:EOAMOA>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR-IIIA; RNA POLYMERASE-II; CRYSTAL-STRUCTURE; BINDING SPECIFICITY; ACTIVATION; SEQUENCE; COMPLEX; DOMAINS; PROMOTER; AFFINITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Sugiura, Y Kyoto Univ, Inst Chem Res, Uji, Kyoto 6110011, Japan Kyoto Univ Uji Kyoto Japan 6110011 , Uji, Kyoto 6110011, Japan
Citazione:
K. Matsushita e Y. Sugiura, "Effect of arginine mutation of alanine-556 on DNA recognition of zinc finger protein Sp1", BIO MED CH, 9(9), 2001, pp. 2259-2267

Abstract

Human transcription factor Spl, which contains three Cys(2)His(2)-class, zinc finger motives, specifically binds to the so-called GC box DNA. It has been indicated that finger I has a unique DNA-binding mode compared with fingers 2 and 3, or the Zif268 model. Therefore, we investigate the role of Ala at position 6 on the recognition helix, which is not responsible for guanine recognition and highly conserved among Spl family. Several Ala-556 mutations of Sp1 bind to DNA with different DNA-binding features. In particular, the Ala --> Arg substitution alters the DNA-binding contribution of the three zinc fingers in Sp1. In this case, the DNA-binding specificity of each finger decreases in the order 2 > 1 > 3. This result reveals that one amino acid in position 6 plays an important role not only for the selectivity to the putative finger 1 subsite, but also for the binding mode of the three fingers to each finger subsite. Probably, Ala-556 is indispensable to characterize the binding mode of the Sp1 zinc fingers, namely the diverse binding contribution of finger 1 and the rigid binding one of finger 3. In Spl,the N-terminal finger 1 serves as a 'hinge finger'. (C) 2001 Elsevier Science Ltd. All rights reserved.

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Documento generato il 10/07/20 alle ore 09:22:45