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Titolo:
Solution structures of the N-terminal domain of histone H-4
Autore:
Bang, E; Lee, CH; Yoon, YB; Lee, DW; Lee, W;
Indirizzi:
Yonsei Univ, Coll Sci, Dept Biochem, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 Biochem, Seoul 120749, South Korea Yonsei Univ, Dept Chem, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 ept Chem, Seoul 120749, South Korea Korea Basic Sci Inst, Seoul Branch, Seoul, South Korea Korea Basic Sci Inst Seoul South Korea Seoul Branch, Seoul, South Korea Yonsei Univ, Coll Sci, Prot Network Res Ctr, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 Res Ctr, Seoul 120749, South Korea
Titolo Testata:
JOURNAL OF PEPTIDE RESEARCH
fascicolo: 5, volume: 58, anno: 2001,
pagine: 389 - 398
SICI:
1397-002X(200111)58:5<389:SSOTND>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR MAGNETIC-RESONANCE; INTERPROTON DISTANCE DATA; PROTEIN BDS-I; 3-DIMENSIONAL STRUCTURES; NMR-SPECTROSCOPY; H-1-NMR SPECTRA; ACETYLATION; YEAST; H4; ACETYLTRANSFERASE;
Keywords:
acetylation; CD; histone; H4; NMR; simulated annealing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Lee, W Yonsei Univ, Coll Sci, Dept Biochem, 134 Shinchon Dong, Seoul 120749, South Korea Yonsei Univ 134 Shinchon Dong Seoul South Korea 120749 South Korea
Citazione:
E. Bang et al., "Solution structures of the N-terminal domain of histone H-4", J PEPT RES, 58(5), 2001, pp. 389-398

Abstract

Histones, nuclear proteins that interact with DNA to form nucleosomes, areessential for both the regulation of transcription and the packaging of DNA within chromosomes. The N-terminal domain of histone H4 contains four acetylation sites at lysine residues and may play a separate role in chromatinstructure from the remainder of the H4 chain. We performed circular dichroism and NMR characterization of both native (H4(NTP)) and acetylated (Ace-H4(NTP)) peptides containing N-terminal acetylation domain of histone H4 forvarious pH environments. Data from CD and NMR suggested that H4 NTP exhibited a pH-dependent conformational change, whereas the Ace-H4(NTP) is insensitive to pH change. However, both peptides showed a defined structural format acidic pH environments. The solution structure for Ace-H4(NTP) shows two structurally independent regions comprising residues of Leu(10)-Gly(13) and Arg(19)-Leu(22), demonstrating relatively well-defined turn-type structures. Our results suggest that N-terminal acetylated region of H4 prefers anextended backbone conformation at neutral pH, however, upon acetylation, the regions containing lysine residues induce structural transition, having defined structural form for its optimum function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:46:59