Structure of SAP18: A Ubiquitin Fold in Histone Deacetylase Complex Assembly

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• 作者：Scott A. McCallum ; J. Fernando Bazan ; Mark Merchant ; JianPing Yin ; Borlan Pan ; Frederic J. de Sauvage ; Wayne J. Fairbrother
• 刊名：Biochemistry
• 出版年：2006
• 出版时间：October 3, 2006
• 年：2006
• 卷：45
• 期：39
• 页码：11974 - 11982
• 全文大小：479K
• 年卷期：v.45,no.39(October 3, 2006)
• ISSN：1520-4995

文摘

Signal transduction pathways are frequently found to repress transcription of target genes inthe absence of stimulation and, conversely, to upregulate transcription in the presence of a signal.Transcription factors are central in this dual regulatory mechanism and widely use a generalized mechanismto repress transcription through recruitment of a Sin3-histone deacetylase (HDAC) complex to theirbinding sites on DNA. The protein SAP18 (Sin3-associated polypeptide of 18 kDa) has been shown toplay a key role in gene-specific recruitment of the HDAC complex by a number of transcription factorsincluding Gli, GAGA, and Bicoid. The solution structure of SAP18 reveals a ubiquitin-like fold withseveral large loop insertions relative to other family members. This fold supports the functional role ofSAP18 as a protein-protein adapter module and provides insight for how SAP18 may bridge the Sin3-HDAC complex to transcription factors.