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Titolo:
ADAPTABILITY AT THE PROTEIN-DNA INTERFACE IS AN IMPORTANT ASPECT OF SEQUENCE RECOGNITION BY BZIP PROTEINS
Autore:
KIM J; TZAMARIAS D; ELLENBERGER T; HARRISON SC; STRUHL K;
Indirizzi:
HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT BIOL CHEM & MOLEC PHARMACOL BOSTON MA 02115 HARVARD UNIV,HOWARD HUGHES MED INST CAMBRIDGE MA 02138 HARVARD UNIV,DEPT BIOCHEM & MOLEC BIOL CAMBRIDGE MA 02138
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 10, volume: 90, anno: 1993,
pagine: 4513 - 4517
SICI:
0027-8424(1993)90:10<4513:AATPII>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
GCN4 ACTIVATOR PROTEIN; LEUCINE ZIPPER; YEAST GCN4; BINDING DOMAIN; SPECIFICITY; FAMILY; C/EBP; DIMER; SITES; JUN;
Keywords:
DNA-BINDING PROTEIN; YEAST GCN4; TRANSCRIPTION FACTOR; GENE REGULATION; LEUCINE ZIPPER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
J. Kim et al., "ADAPTABILITY AT THE PROTEIN-DNA INTERFACE IS AN IMPORTANT ASPECT OF SEQUENCE RECOGNITION BY BZIP PROTEINS", Proceedings of the National Academy of Sciences of the United Statesof America, 90(10), 1993, pp. 4513-4517

Abstract

The related AP-1 and ATF/CREB families of transcriptional regulatory proteins bind as dimers to overlapping or adjacent DNA half-sites by using a bZIP structural motif. Using genetic selections, we isolate derivatives of yeast GCN4 that affect DNA-binding specificity at particular positions of the AP-1 target sequence. In general, altered DNA-binding specificity results from the substitution of larger hydrophobic amino acids for GCN4 residues that contact base pairs. However, in several cases, DNA binding by the mutant proteins cannot be simply explained in terms of the GCN4-AP-1 structure; movement of the protein and/or DNA structural changes are required to accommodate the amino acid substitutions. The quintet of GCN4 residues that make base-pair contacts do not entirely determine DNA-binding specificity because these residues are highly conserved in the bZIP family, yet many of the bZIP proteins bind to distinct DNA sites. The alpha-helical fork between the GCN4DNA-binding and dimerization surfaces is important for half-site spacing preferences, because mutations in the fork alter the relative affinity for AP-1 and ATF/CREB sites. The basic region in the protein-DNA complex is a long isolated alpha-helix, with no constraints from otherparts of a folded domain. From all of these considerations, we suggest that small shifts in position and orientation or local deformations in the alpha-helical backbone distinguish one bZIP complex from another.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 04:34:18