| http://purl.uniprot.org/citations/31147444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31147444 | http://www.w3.org/2000/01/rdf-schema#comment | "AF4/FMR2 family member 4 (AFF4) is the scaffold protein of the multisubunit super-elongation complex, which plays key roles in the release of RNA polymerase II from promoter-proximal pausing and in the transactivation of HIV-1 transcription. AFF4 consists of an intrinsically disordered N-terminal region that interacts with other super-elongation complex subunits and a C-terminal homology domain (CHD) that is conserved among AF4/FMR2 family proteins, including AFF1, AFF2, AFF3, and AFF4. Here, we solved the X-ray crystal structure of the CHD in human AFF4 (AFF4-CHD) to 2.2 Å resolution and characterized its biochemical properties. The structure disclosed that AFF4-CHD folds into a novel domain that consists of eight helices and is distantly related to tetratrico peptide repeat motifs. Our analyses further revealed that AFF4-CHD mediates the formation of an AFF4 homodimer or an AFF1-AFF4 heterodimer. Results from fluorescence anisotropy experiments suggested that AFF4-CHD interacts with both RNA and DNA in vitro Furthermore, we identified a surface loop region in AFF4-CHD as a substrate for the P-TEFb kinase cyclin-dependent kinase 9, which triggers release of polymerase II from promoter-proximal pausing sites. In conclusion, the AFF-CHD structure and biochemical analyses reported here reveal the molecular basis for the homo- and heterodimerization of AFF proteins and implicate the AFF4-CHD in nucleic acid interactions. The high conservation of the CHD among several other proteins suggests that our results are also relevant for understanding other CHD-containing proteins and their dimerization behavior."xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.ra119.008577"xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/author | "Cramer P."xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/pages | "10663-10673"xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/title | "Structure of the super-elongation complex subunit AFF4 C-terminal homology domain reveals requirements for AFF homo- and heterodimerization."xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://purl.uniprot.org/core/volume | "294"xsd:string |
| http://purl.uniprot.org/citations/31147444 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31147444 |
| http://purl.uniprot.org/citations/31147444 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31147444 |
| http://purl.uniprot.org/uniprot/#_Q8TAX5-mappedCitation-31147444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31147444 |
| http://purl.uniprot.org/uniprot/#_Q7Z2T0-mappedCitation-31147444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31147444 |
| http://purl.uniprot.org/uniprot/#_Q9UHB7-mappedCitation-31147444 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31147444 |
| http://purl.uniprot.org/uniprot/Q9UHB7 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/31147444 |
| http://purl.uniprot.org/uniprot/Q7Z2T0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/31147444 |
| http://purl.uniprot.org/uniprot/Q8TAX5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/31147444 |