8jj6

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Structure of the NELF-BCE complex

Structural highlights

8jj6 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.72Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NELFB_HUMAN Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, binds weakly to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1. May be able to induce chromatin unfolding.[1] [2] [3] [4]

Publication Abstract from PubMed

Negative elongation factor (NELF) is a four-subunit transcription elongation factor that mainly functions in maintaining the paused state of RNA polymerase II in eukaryotes. Upon binding to Pol II, NELF works synergistically with DRB sensitivity-inducing factor (DSIF) and inhibits transcription elongation of Pol II, which subsequently retains a stably paused state 20-60 base pairs downstream of the promoter. The promoter-proximal pausing of Pol II caused by NELF is a general mechanism of transcriptional regulation for most signal-responsive genes. To date, structural studies have significantly advanced our understanding of the molecular mechanisms of NELF. However, a high quality structural model clarifying the interaction details of this complex is still lacking. In this study, we solved the high resolution crystal structure of the NELF-B/C/E ternary complex. We observed detailed interactions between subunits and identified residues important for the association between NELF-B and NELF-E. Our work presents a precise model of the NELF complex, which will facilitate our understanding of its in vivo function.

Structural basis of the human negative elongation factor NELF-B/C/E ternary complex.,Cao Y, Qin Y, Zhang W, Tian W, Ren Y, Ren J, Wang J, Wang M, Jiang J, Wang Z Biochem Biophys Res Commun. 2023 Oct 15;677:155-161. doi: , 10.1016/j.bbrc.2023.08.019. Epub 2023 Aug 10. PMID:37591184[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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Distinct negative elongation factor conformations regulate RNA polymerase II promoter-proximal pausing.
Su et al. (2024)
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References

  1. ↑ Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell. 1999 Apr 2;97(1):41-51. PMID:10199401
  2. ↑ Narita T, Yamaguchi Y, Yano K, Sugimoto S, Chanarat S, Wada T, Kim DK, Hasegawa J, Omori M, Inukai N, Endoh M, Yamada T, Handa H. Human transcription elongation factor NELF: identification of novel subunits and reconstitution of the functionally active complex. Mol Cell Biol. 2003 Mar;23(6):1863-73. PMID:12612062
  3. ↑ Natarajan M, Schiralli Lester GM, Lee C, Missra A, Wasserman GA, Steffen M, Gilmour DS, Henderson AJ. Negative elongation factor (NELF) coordinates RNA polymerase II pausing, premature termination, and chromatin remodeling to regulate HIV transcription. J Biol Chem. 2013 Sep 6;288(36):25995-6003. doi: 10.1074/jbc.M113.496489. Epub, 2013 Jul 24. PMID:23884411 doi:http://dx.doi.org/10.1074/jbc.M113.496489
  4. ↑ Vos SM, Pollmann D, Caizzi L, Hofmann KB, Rombaut P, Zimniak T, Herzog F, Cramer P. Architecture and RNA binding of the human negative elongation factor. Elife. 2016 Jun 10;5. pii: e14981. doi: 10.7554/eLife.14981. PMID:27282391 doi:http://dx.doi.org/10.7554/eLife.14981
  5. ↑ Cao Y, Qin Y, Zhang W, Tian W, Ren Y, Ren J, Wang J, Wang M, Jiang J, Wang Z. Structural basis of the human negative elongation factor NELF-B/C/E ternary complex. Biochem Biophys Res Commun. 2023 Oct 15;677:155-161. PMID:37591184 doi:10.1016/j.bbrc.2023.08.019

Contents


PDB ID 8jj6

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OCA

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