期刊
BIOCHEMISTRY
卷 45, 期 1, 页码 121-130出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi051787e
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资金
- NCI NIH HHS [T32 CA009385-21, T32 CA009385, T32CA09385] Funding Source: Medline
- NIEHS NIH HHS [P30 ES000267-37, P30 ES000267, P30 ES000267-38] Funding Source: Medline
- NIGMS NIH HHS [R01 GM062112-05, R01 GM075156-01, R01 GM055420, T32 GM008320, T32 GM008320-12, R01 GM055420-11, R01 GM062112-04, R01GM55420, R01 GM075156, R01GM62112, R01 GM062112-03, R01 GM062112, R01 GM055420-12, T32GM08320, T32 GM008320-13, R01GM75156] Funding Source: Medline
Prp19 is an essential splicing factor and a member of the U-box family of E3 ubiquitin ligases. Prp19 forms a tetramer via a central coiled-coil domain. Here, we show the U-box domain of Prp19 exists as a dimer within the context of the Prp19 tetramer. A high-resolution structure of the homodimeric state of the Prp19 U-box was determined by X-ray crystallography. Mutation of the U-box dimer interface abrogates U-box dimer formation and is lethal in vivo. The structure of the U-box dimer enables construction of a complete model of Prp19 providing insights into how the tetrameric protein functions as an E3 ligase. Finally, comparison of the Prp19 U-box homodimer with the heterodimeric complex of BRCA1/ BARD1 RLNG-finger domains uncovers a common architecture for a family of oligomeric U-box and RING-finger E3 ubiquitin ligases, which has mechanistic implications for E3 ligase-mediated polyubiquitination and E4 polyubiquitin ligases.
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