期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 292, 期 16, 页码 6431-6437出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C117.777946
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资金
- Helen Nelson Medical Research Fund at the Greater Kansas City Community Foundation
- Francis Crick Institute from Cancer Research UK [FC001166]
- UK Medical Research Council [FC001166]
- Wellcome Trust [FC001166]
- European Research Council [693327, 268797]
- European Research Council (ERC) [268797] Funding Source: European Research Council (ERC)
- Cancer Research UK [11567] Funding Source: researchfish
- The Francis Crick Institute [10490, 10002, 10168, 10166] Funding Source: researchfish
- Grants-in-Aid for Scientific Research [15K08177] Funding Source: KAKEN
Elongin A performs dual functions as the transcriptionally active subunit of RNA polymerase II (Pol II) elongation factor Elongin and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase that ubiquitylates Pol II in response to DNA damage. Assembly of the ElonginAubiquitin ligase and its recruitment to sites ofDNAdamage is a tightly regulated process induced by DNA-damaging agents and alpha-amanitin, a drug that induces Pol II stalling. In this study, we demonstrate (i) that Elongin A and the ubiquitin ligase subunit CUL5 associate in cells with the Cockayne syndrome B (CSB) protein and (ii) that this interaction is also inducedbyDNA-damagingagentsand alpha-amanitin. Inaddition, we presentevidencethattheCSBproteinpromotesstablerecruitment of the ElonginAubiquitin ligase to sites ofDNAdamage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and theCSBprotein function together in acommonpathway in response to Pol II stalling and DNA damage.
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