Structure of the super-elongation complex subunit AFF4 C-terminal homology domain reveals requirements for AFF homo- and heterodimerization.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
05 07 2019
Historique:
received: 01 04 2019
revised: 27 05 2019
pubmed: 31 5 2019
medline: 11 3 2020
entrez: 1 6 2019
Statut: ppublish

Résumé

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

Identifiants

pubmed: 31147444
pii: S0021-9258(20)31855-X
doi: 10.1074/jbc.RA119.008577
pmc: PMC6615702
doi:

Substances chimiques

AFF4 protein, human 0
Protein Subunits 0
Recombinant Proteins 0
Transcriptional Elongation Factors 0
RNA 63231-63-0
DNA 9007-49-2
Positive Transcriptional Elongation Factor B EC 2.7.11.-

Banques de données

PDB
['6GKG-F']

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

10663-10673

Informations de copyright

© 2019 Chen and Cramer.

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Auteurs

Ying Chen (Y)

From the Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Patrick Cramer (P)

From the Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany patrick.cramer@mpibpc.mpg.de.

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Classifications MeSH