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Titolo:
FUNCTIONAL INTERACTION OF THE C-MYC TRANSACTIVATION DOMAIN WITH THE TATA-BINDING PROTEIN - EVIDENCE FOR AN INDUCED FIT MODEL OF TRANSACTIVATION DOMAIN FOLDING
Autore:
MCEWAN IJ; DAHLMANWRIGHT K; FORD J; WRIGHT APH;
Indirizzi:
KAROLINSKA INST,NOVUM,DEPT BIOSCI,CTR BIOTECHNOL S-14157 HUDDINGE SWEDEN
Titolo Testata:
Biochemistry
fascicolo: 29, volume: 35, anno: 1996,
pagine: 9584 - 9593
SICI:
0006-2960(1996)35:29<9584:FIOTCT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; EUKARYOTIC TRANSCRIPTIONAL ACTIVATORS; HUMAN GLUCOCORTICOID RECEPTOR; RETINOBLASTOMA GENE-PRODUCT; N-TERMINAL DOMAIN; DNA-BINDING; INITIATION-FACTOR; NEOPLASTIC TRANSFORMATION; BASAL TRANSCRIPTION; BURKITTS-LYMPHOMA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
85
Recensione:
Indirizzi per estratti:
Citazione:
I.J. Mcewan et al., "FUNCTIONAL INTERACTION OF THE C-MYC TRANSACTIVATION DOMAIN WITH THE TATA-BINDING PROTEIN - EVIDENCE FOR AN INDUCED FIT MODEL OF TRANSACTIVATION DOMAIN FOLDING", Biochemistry, 35(29), 1996, pp. 9584-9593

Abstract

c-Myc is a member of a family of sequence specific-DNA binding proteins that are thought to regulate tile transcription of genes involved in normal cell growth, differentiation, and apoptosis. In order to understand how human c-myc functions as a transcription factor, we have studied the mechanism of action and structure of the N-terminal transactivation domain, amino acids 1-143. In a protein interaction assay-, c-myc(1-143) bound selectively to two basal transcription factors, the TATA binding protein (TBP) and the RAP74 subunit of TFIIF. Furthermore,the isolated c-myc transactivation domain competed for limiting factors required the assembly of a functional preinitiation complex. This squelching of basal transcription was reversed in a dose,dependent manner by recombinant TBP. Taken together, these results identify TBP as an important target for the c-myc transactivation domain, during transcriptional initiation. Similar to other transactivation domains, the c-myc(1-143) polypeptide showed little or no evidence of secondary structure, when measured by circular dichroism spectroscopy (CD) in aqueoussolution. However, significant alpha-helical conformation was observed in the presence of the hydrophobic solvent trifluoroethanol. Strikingly, addition of TBP caused changes in the CD spectra consistent with induction of protein conformation in c-myc(1-143) during interaction with the target factor. This change was specific for TBP as a similar effect was not observed in the presence of TFIIB, These data support a model in which target factors induce or stabilize a structural conformation in activator proteins during transcriptional transactivation.

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Documento generato il 26/11/20 alle ore 20:34:06