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Titolo:
HETERODIMERIZATION OF THE YEAST HOMEODOMAIN TRANSCRIPTIONAL REGULATORS ALPHA-2 AND A1 - SECONDARY STRUCTURE DETERMINATION OF THE A1 HOMEODOMAIN AND CHANGES PRODUCED BY ALPHA-2 INTERACTIONS
Autore:
BAXTER SM; GONTRUM DM; PHILLIPS CL; ROTH AF; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97404 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97404
Titolo Testata:
Biochemistry
fascicolo: 51, volume: 33, anno: 1994,
pagine: 15309 - 15320
SICI:
0006-2960(1994)33:51<15309:HOTYHT>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; COUPLING-CONSTANTS 3JHN-ALPHA; HUMAN PROTOONCOGENE PBX1; DNA-BINDING SPECIFICITY; HOMEO DOMAIN PROTEIN; ANTENNAPEDIA HOMEODOMAIN; NMR-SPECTROSCOPY; CRYSTAL-STRUCTURE; COMPLEX; PROTON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
S.M. Baxter et al., "HETERODIMERIZATION OF THE YEAST HOMEODOMAIN TRANSCRIPTIONAL REGULATORS ALPHA-2 AND A1 - SECONDARY STRUCTURE DETERMINATION OF THE A1 HOMEODOMAIN AND CHANGES PRODUCED BY ALPHA-2 INTERACTIONS", Biochemistry, 33(51), 1994, pp. 15309-15320

Abstract

The homeodomain proteins, a1 and alpha 2, act cooperatively to regulate cell-type specific genes in yeast. The basis of this cooperativity is an interaction between the two proteins, forming a heterodimer thatbinds DNA tightly and specifically. A fragment containing the homeodomain of al, a1(66-126), has been studied by NMR spectroscopy to gain secondary structure information and to characterize the changes in al upon heterodimerization with alpha 2. Heteronuclear (H-1-N-15) NMR methods were used to assign backbone resonances of the 61 amino acid fragment. The a1(66-126) secondary structure was determined using NOE connectivities, (3)J(HN alpha), coupling constants and hydrogen exchange kinetic data. NMR data identify three helical segments separated by a loop and a tight turn that are the characteristic structural elements ofhomeodomain proteins. The al fragment was titrated with alpha 2(128-210), the homeodomain-containing fragment of alpha 2, to study changes in a1(66-126) spectra produced by alpha 2 binding. The a1(66-126) protein was labeled with N-15 and selectively observed using isotope-edited NMR experiments. NMR spectra of bound a1(66-126) indicate that residues in helix 1, helix 2, and the loop connecting them are directly involved in the binding of the alpha 2 fragment. Relatively minor effectson the resonances from residues in helix 3, the putative DNA-binding helix, were noted upon alpha 2 binding. We have thus located a region of the al homeodomain important for specific protein recognition.

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Documento generato il 07/07/20 alle ore 17:32:56