PubMed:9859997 JSONTXT

Annnotations TAB JSON ListView MergeView

    relna

    {"project":"relna","denotations":[{"id":"T1","span":{"begin":51,"end":57},"obj":"DNA"},{"id":"T2","span":{"begin":463,"end":468},"obj":"Protein"},{"id":"T3","span":{"begin":470,"end":474},"obj":"Protein"},{"id":"T4","span":{"begin":476,"end":486},"obj":"Protein"},{"id":"T5","span":{"begin":491,"end":495},"obj":"DNA"},{"id":"T6","span":{"begin":496,"end":499},"obj":"DNA"},{"id":"T7","span":{"begin":569,"end":578},"obj":"Protein"},{"id":"T8","span":{"begin":580,"end":585},"obj":"Protein"},{"id":"T9","span":{"begin":587,"end":591},"obj":"DNA"},{"id":"T10","span":{"begin":596,"end":599},"obj":"DNA"},{"id":"T11","span":{"begin":602,"end":608},"obj":"DNA"},{"id":"T12","span":{"begin":810,"end":814},"obj":"DNA"},{"id":"T13","span":{"begin":815,"end":818},"obj":"DNA"},{"id":"T14","span":{"begin":840,"end":846},"obj":"DNA"},{"id":"T15","span":{"begin":873,"end":877},"obj":"DNA"},{"id":"T16","span":{"begin":922,"end":928},"obj":"DNA"},{"id":"T17","span":{"begin":969,"end":975},"obj":"DNA"},{"id":"T18","span":{"begin":1032,"end":1038},"obj":"DNA"},{"id":"T19","span":{"begin":1040,"end":1046},"obj":"DNA"},{"id":"T20","span":{"begin":1110,"end":1116},"obj":"DNA"},{"id":"T21","span":{"begin":1270,"end":1276},"obj":"DNA"}],"relations":[{"id":"R0","pred":"linked","subj":"T4","obj":"T9"}],"text":"Regulation of activity of the transcription factor GATA-1 by acetylation.\nModification of histones, DNA-binding proteins found in chromatin, by addition of acetyl groups occurs to a greater degree when the histones are associated with transcriptionally active DNA. A breakthrough in understanding how this acetylation is mediated was the discovery that various transcriptional co-activator proteins have intrinsic histone acetyltransferase activity (for example, Gcn5p, PCAF, TAF(II)250 and p300/CBP. These acetyltransferases also modify certain transcription factors (TFIIEbeta, TFIIF, EKLF and p53). GATA-1 is an important transcription factor in the haematopoietic lineage and is essential for terminal differentiation of erythrocytes and megakaryocytes. It is associated in vivo with the acetyltransferase p300/CBP. Here we report that GATA-1 is acetylated in vitro by p300. This significantly increases the amount of GATA-1 bound to DNA and alters the mobility of GATA-1-DNA complexes, suggestive of a conformational change in GATA-1. GATA-1 is also acetylated in vivo and acetylation directly stimulates GATA-1-dependent transcription. Mutagenesis of important acetylated residues shows that there is a relationship between the acetylation and in vivo function of GATA-1. We propose that acetylation of transcription factors can alter interactions between these factors and DNA and among different transcription factors, and is an integral part of transcription and differentiation processes."}