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Titolo:
TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells
Autore:
Chung, MC; Kim, HK; Kawamoto, S;
Indirizzi:
NHLBI, Mol Cardiol Lab, NIH, Bethesda, MD 20892 USA NHLBI Bethesda MD USA20892 Mol Cardiol Lab, NIH, Bethesda, MD 20892 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 30, volume: 40, anno: 2001,
pagine: 8887 - 8897
SICI:
0006-2960(20010731)40:30<8887:TCFAAT>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOOP-HELIX PROTEIN; FACTOR USF; MESSENGER-RNA; NUCLEAR-LOCALIZATION; REGULATORY PROTEINS; CELLULAR MYOSIN; DNA-BINDING; MYOD FAMILY; CLONING; DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Kawamoto, S NHLBI, Mol Cardiol Lab, NIH, Bldg 10,Room 8N202,10 Ctr Dr,MSC 1762, Bethesda, MD 20892 USA NHLBI Bldg 10,Room 8N202,10 Ctr Dr,MSC 1762 Bethesda MD USA 20892
Citazione:
M.C. Chung et al., "TFEC can function as a transcriptional activator of the nonmuscle myosin II heavy chain-A gene in transfected cells", BIOCHEM, 40(30), 2001, pp. 8887-8897

Abstract

Transcription of the human nonmuscle myosin II heavy chain-A (NMHC-A) geneis regulated via multiple elements located in intron I, including element F which contains an E-box. In this study we have identified and characterized the factors that are capable of binding to element F. Yeast one-hybrid screening using element F allowed isolation of cDNAs encoding transcriptional factors TFEC, TFE3, and USF2, each of which contains basic helix-loop-helix and leucine zipper motifs. Furthermore, cDNA cloning by polymerase chainreaction yielded cDNAs for two TFEC isoforms, designated TFEC-1 and TFEC-s, which are generated by alternative pre-mRNA splicing. In addition to these four factors, USF1, which is known to share the same DNA binding elementswith USF2, was isolated for comparison. Electrophoretic mobility shift assays and cotransfection studies of the expression constructs with reporter gene constructs revealed that the above five factors have different binding activities for element F with different transactivation potencies. USF1 andUSF2 demonstrate the highest binding activity to element F, yet show the lowest element F-dependent transactivation. TFE3 has a high transactivation potency but the lowest binding activity. TFEC-1 demonstrates a high bindingactivity with the highest transactivation potency, whereas TFEC-s has the same binding activity as TFEC-1 with intermediate transactivation. We also demonstrate that an N-terminal activation domain exists only in TFEC-1, whereas a C-terminal activation domain is common to both the 1 and s isoforms. This study provides the first evidence of TFEC being an activator of transcription, with two separate activation domains.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 11:22:19