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Titolo:
CHARACTERIZATION OF AN ACETYLCHOLINE-RECEPTOR ALPHA-3 GENE PROMOTER AND ITS ACTIVATION BY THE POU DOMAIN FACTOR SCIP TST-1/
Autore:
YANG XD; MCDONOUGH J; FYODOROV D; MORRIS M; WANG F; DENERIS ES;
Indirizzi:
CASE WESTERN RESERVE UNIV,SCH MED,DEPT NEUROSCI,2109 ADELBERT RD CLEVELAND OH 44106 CASE WESTERN RESERVE UNIV,SCH MED,DEPT NEUROSCI CLEVELAND OH 44106
Titolo Testata:
The Journal of biological chemistry
fascicolo: 14, volume: 269, anno: 1994,
pagine: 10252 - 10264
SICI:
0021-9258(1994)269:14<10252:COAAAG>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
CENTRAL-NERVOUS-SYSTEM; CHICK CILIARY GANGLIA; RAT CENTRAL NEURONS; TRANSCRIPTION FACTOR; NICOTINIC RECEPTOR; HOMEOBOX GENE; FUNCTIONAL DIVERSITY; CPG ISLANDS; EXPRESSION; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
74
Recensione:
Indirizzi per estratti:
Citazione:
X.D. Yang et al., "CHARACTERIZATION OF AN ACETYLCHOLINE-RECEPTOR ALPHA-3 GENE PROMOTER AND ITS ACTIVATION BY THE POU DOMAIN FACTOR SCIP TST-1/", The Journal of biological chemistry, 269(14), 1994, pp. 10252-10264

Abstract

Genes encoding neuronal nicotinic acetylcholine receptors exhibit restricted patterns of expression in the nervous system. We are interested in elucidating the molecular mechanisms responsible for establishingthese patterns of expression. This paper presents the characterization of regulatory elements upstream of the neuronal nicotinic acetylcholine receptor alpha 3 gene. We have identified a GC-rich multistart site promoter adjacent to the alpha 3 coding region. Similar alpha 3 start sites were identified in PC12 cells and sympathetic ganglion neurons, suggesting similar control mechanisms in the clonal line and peripheral neurons. The start site region lacks TATA-like sequences but does contain initiator-like sequences. We show in transient transfection assays, that the POU domain transcription factor, SCI/Tst-1, specifically activates alpha 3 in a neural context. Other POU domain factors tested only weakly activated or repressed alpha 3. Unexpectedly, we found that alpha 3 basal activity and SCIP/Tst-1 activation of alpha 3 is not dependent on the SCIP/Tst-1 binding sites found upstream of the gene. In addition, mutations in the SCIP/Tst-1 coding region that prevent the factor from binding to DNA with high affinity do not obliterate alpha 3 activation. These results lead us to propose that alpha 3 activation by SCIP/Tst-1 is achieved via protein-protein interactions between SCIP/Tst-1 and a specific complement of transcription factors that act directly on the promoter.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 15:39:07