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Titolo:
CONSERVATIVE VAL(47) RESIDUE OF POU HOMEODOMAIN - ROLE IN DNA RECOGNITION
Autore:
STEPCHENKO AG; LUCHINA NN; POLANOVSKY OL;
Indirizzi:
RUSSIAN ACAD SCI,VA ENGELHARDT MOL BIOL INST,VAVILOV STR 32 MOSCOW 117984 RUSSIA
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 412, anno: 1997,
pagine: 5 - 8
SICI:
0014-5793(1997)412:1<5:CVROPH>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; BINDING DOMAIN; TRANSCRIPTION; OCT-1; SPECIFICITY; SUGGESTS; PROTEIN;
Keywords:
OCT-2 PROTEIN; POU DOMAIN MUTANTS; OCT-SEQUENCE; HOMEO-SPECIFIC SITE; PROTEIN-DNA RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
20
Recensione:
Indirizzi per estratti:
Citazione:
A.G. Stepchenko et al., "CONSERVATIVE VAL(47) RESIDUE OF POU HOMEODOMAIN - ROLE IN DNA RECOGNITION", FEBS letters, 412(1), 1997, pp. 5-8

Abstract

Conservative Val(47) residue, located in the third recognition helix of the Oct-2 POU domain, was alternately substituted with other 19 amino acids. Affinity and specificity of interaction with oct-site ATGCAAANGA and homeo-specific site ATAANGA mere determined for all mutants. The wild type protein (with Val(47)) has maximal affinity and specificity in POU domain interaction with octamer sequence. However, V47I mutant showed stronger interaction with homeo-specific site. The highest specificity of interaction with homeo-site was recorded for V47S mutant. We conclude that only Val(47) provides sequence-specific high-affinity binding of POU proteins with octamer targets other than the homeo-specific site. It is shown also that damages caused by point mutationsmay be at least partially compensated by participation in the oct-site recognition of both POUh and POUs domains. (C) 1997 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 15:29:16