English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Architecture and RNA binding of the human negative elongation factor.

MPS-Authors
/persons/resource/persons196569

Vos,  S. M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons188037

Pöllmann,  D.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons191504

Caizzi,  L.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons196571

Hofmann,  K. B.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons127020

Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

External Ressource
Fulltext (public)

2305918.pdf
(Publisher version), 7MB

Supplementary Material (public)

2305918-Suppl.pdf
(Supplementary material), 11MB

Citation

Vos, S. M., Pöllmann, D., Caizzi, L., Hofmann, K. B., Rombaut, P., Zimniak, T., et al. (2016). Architecture and RNA binding of the human negative elongation factor. eLife, 5: e14981. doi:10.7554/eLife.14981.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-E444-1
Abstract
Transcription regulation in metazoans often involves promoter-proximal pausing of RNA polymerase (Pol) II, which requires the 4-subunit negative elongation factor (NELF). Here we discern the functional architecture of human NELF through X-ray crystallography, protein crosslinking, biochemical assays, and RNA crosslinking in cells. We identify a NELF core subcomplex formed by conserved regions in subunits NELF-A and NELF-C, and resolve its crystal structure. The NELF-AC subcomplex binds single-stranded nucleic acids in vitro, and NELF-C associates with RNA in vivo. A positively charged face of NELF-AC is involved in RNA binding, whereas the opposite face of the NELF-AC subcomplex binds NELF-B. NELF-B is predicted to form a HEAT repeat fold, also binds RNA in vivo, and anchors the subunit NELF-E, which is confirmed to bind RNA in vivo. These results reveal the three-dimensional architecture and three RNA-binding faces of NELF.