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Structural highlights
Function
NUSA_ECOLI Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.[1] [2] [3] [4] [5] [6] [7] [8] [9]
Publication Abstract from PubMed
Bacteriophage lambdaN protein, a model anti-termination factor, binds nascent RNA and host Nus factors, rendering RNA polymerase resistant to all pause and termination signals. A 3.7-A-resolution cryo-electron microscopy structure and structure-informed functional analyses reveal a multi-pronged strategy by which the intrinsically unstructured lambdaN directly modifies RNA polymerase interactions with the nucleic acids and subverts essential functions of NusA, NusE, and NusG to reprogram the transcriptional apparatus. lambdaN repositions NusA and remodels the beta subunit flap tip, which likely precludes folding of pause or termination RNA hairpins in the exit tunnel and disrupts termination-supporting interactions of the alpha subunit C-terminal domains. lambdaN invades and traverses the RNA polymerase hybrid cavity, likely stabilizing the hybrid and impeding pause- or termination-related conformational changes of polymerase. lambdaN also lines upstream DNA, seemingly reinforcing anti-backtracking and anti-swiveling by NusG. Moreover, lambdaN-repositioned NusA and NusE sequester the NusG C-terminal domain, counteracting rho-dependent termination. Other anti-terminators likely utilize similar mechanisms to enable processive transcription.
Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor.,Krupp F, Said N, Huang YH, Loll B, Burger J, Mielke T, Spahn CMT, Wahl MC Mol Cell. 2019 Feb 12. pii: S1097-2765(19)30036-X. doi:, 10.1016/j.molcel.2019.01.016. PMID:30795892[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Greenblatt J, Li J. Interaction of the sigma factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcription. Cell. 1981 May;24(2):421-8. PMID:6263495
- ↑ Greenblatt J, McLimont M, Hanly S. Termination of transcription by nusA gene protein of Escherichia coli. Nature. 1981 Jul 16;292(5820):215-20. PMID:6265785
- ↑ Schmidt MC, Chamberlin MJ. Amplification and isolation of Escherichia coli nusA protein and studies of its effects on in vitro RNA chain elongation. Biochemistry. 1984 Jan 17;23(2):197-203. PMID:6199039
- ↑ Schmidt MC, Chamberlin MJ. nusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites. J Mol Biol. 1987 Jun 20;195(4):809-18. PMID:2821282 doi:https://dx.doi.org/10.1016/0022-2836(87)90486-4
- ↑ Liu K, Hanna MM. NusA contacts nascent RNA in Escherichia coli transcription complexes. J Mol Biol. 1995 Apr 7;247(4):547-58. PMID:7536848 doi:https://dx.doi.org/10.1006/jmbi.1994.0161
- ↑ Vogel U, Jensen KF. NusA is required for ribosomal antitermination and for modulation of the transcription elongation rate of both antiterminated RNA and mRNA. J Biol Chem. 1997 May 9;272(19):12265-71. PMID:9139668
- ↑ Gusarov I, Nudler E. Control of intrinsic transcription termination by N and NusA: the basic mechanisms. Cell. 2001 Nov 16;107(4):437-49. PMID:11719185
- ↑ Cohen SE, Lewis CA, Mooney RA, Kohanski MA, Collins JJ, Landick R, Walker GC. Roles for the transcription elongation factor NusA in both DNA repair and damage tolerance pathways in Escherichia coli. Proc Natl Acad Sci U S A. 2010 Aug 31;107(35):15517-22. doi:, 10.1073/pnas.1005203107. Epub 2010 Aug 9. PMID:20696893 doi:https://dx.doi.org/10.1073/pnas.1005203107
- ↑ Burmann BM, Rosch P. The role of E. coli Nus-factors in transcription regulation and transcription:translation coupling: From structure to mechanism. Transcription. 2011 May;2(3):130-134. PMID:21922055 doi:https://dx.doi.org/10.4161/trns.2.3.15671
- ↑ Krupp F, Said N, Huang YH, Loll B, Burger J, Mielke T, Spahn CMT, Wahl MC. Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor. Mol Cell. 2019 Feb 12. pii: S1097-2765(19)30036-X. doi:, 10.1016/j.molcel.2019.01.016. PMID:30795892 doi:https://dx.doi.org/10.1016/j.molcel.2019.01.016
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