8E82
Mycobacterium tuberculosis RNAP elongation complex with NusG transcription factor
Summary for 8E82
| Entry DOI | 10.2210/pdb8e82/pdb |
| EMDB information | 27942 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total) |
| Functional Keywords | rna polymerase, transcription factor, elongation, pausing, transcription-transferase-dna complex, transcription-dna-rna complex, transcription/dna/rna |
| Biological source | Mycobacterium tuberculosis More |
| Total number of polymer chains | 9 |
| Total formula weight | 428994.52 |
| Authors | Delbeau, M.,Darst, S.A.,Campbell, E.A. (deposition date: 2022-08-25, release date: 2023-03-22, Last modification date: 2024-11-13) |
| Primary citation | Delbeau, M.,Omollo, E.O.,Froom, R.,Koh, S.,Mooney, R.A.,Lilic, M.,Brewer, J.J.,Rock, J.,Darst, S.A.,Campbell, E.A.,Landick, R. Structural and functional basis of the universal transcription factor NusG pro-pausing activity in Mycobacterium tuberculosis. Mol.Cell, 83:1474-1488.e8, 2023 Cited by PubMed Abstract: Transcriptional pauses mediate regulation of RNA biogenesis. DNA-encoded pause signals trigger pausing by stabilizing RNA polymerase (RNAP) swiveling and inhibiting DNA translocation. The N-terminal domain (NGN) of the only universal transcription factor, NusG/Spt5, modulates pausing through contacts to RNAP and DNA. Pro-pausing NusGs enhance pauses, whereas anti-pausing NusGs suppress pauses. Little is known about pausing and NusG in the human pathogen Mycobacterium tuberculosis (Mtb). We report that MtbNusG is pro-pausing. MtbNusG captures paused, swiveled RNAP by contacts to the RNAP protrusion and nontemplate-DNA wedged between the NGN and RNAP gate loop. In contrast, anti-pausing Escherichia coli (Eco) NGN contacts the MtbRNAP gate loop, inhibiting swiveling and pausing. Using CRISPR-mediated genetics, we show that pro-pausing NGN is required for mycobacterial fitness. Our results define an essential function of mycobacterial NusG and the structural basis of pro- versus anti-pausing NusG activity, with broad implications for the function of all NusG orthologs. PubMed: 37116494DOI: 10.1016/j.molcel.2023.04.007 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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