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Titolo:
Npw38, a novel nuclear protein possessing a WW domain capable of activating basal transcription
Autore:
Komuro, A; Saeki, N; Kato, S;
Indirizzi:
ERATO, Japan Sci & Technol Corp, Kato Cytoprot Network Project, Sagami Chem ERATO Sagamihara Kanagawa Japan 2290012 prot Network Project, Sagami Chem
Titolo Testata:
NUCLEIC ACIDS RESEARCH
fascicolo: 9, volume: 27, anno: 1999,
pagine: 1957 - 1965
SICI:
0305-1048(19990501)27:9<1957:NANNPP>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; YES-ASSOCIATED PROTEIN; C-TERMINAL DOMAIN; MESSENGER-RNA; BINDING-PROTEINS; LARGE SUBUNIT; CDNA CLONING; INTERACTS; MOTIF; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Kato, S ERATO, Japan Sci & Technol Corp, Kato Cytoprot Network Project, Sagami Chem ERATO Nishi Ohnuma 4-4-1 Sagamihara Kanagawa Japan 2290012 mi Chem
Citazione:
A. Komuro et al., "Npw38, a novel nuclear protein possessing a WW domain capable of activating basal transcription", NUCL ACID R, 27(9), 1999, pp. 1957-1965

Abstract

We have found a navel cDNA encoding a 265 amino acid protein possessing a WW domain in our full-length cDNA bank. The WW domain was sandwiched between an acidic region and an acidic-basic amino acid repetitive region. In vitro transcription/translation of the cDNA produced a 38 kDa product that wasalso found in the cell lysate by western blot analysis. Thus this protein is named the nuclear protein containing a WW domain with a molecular mass of 38 kDa, Npw38. Immunofluorescence studies and expression of a fusion protein to a green fluorescent protein revealed that this protein is localized in the nucleus. Npw38 was shown to be capable of binding to a poly(rG) resin. Interestingly, the WW domain of Npw38 was found to function as a transcriptional activator in CHO cells using the GAL4 DNA-binding fusion system. Furthermore, the WW domains of human YAP and Pin1 were demonstrated to have a similar transcription-promoting activity. Combined mutation of the conserved first and second Trp residues and a hydrophobic triplet of TyrTyrTrp inthe WW domain of Npw38 abolished the transcription-promoting activity, butsingle mutations of these sites did not. These results suggest that some WW domains potentially possess transcription-promoting activity in mammaliancells.

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Documento generato il 30/11/20 alle ore 17:26:41