6YI2

UvrD helicase RNA polymerase interactions are governed by UvrDs carboxy terminal Tudor domain.

Summary for 6YI2

• Entry DOI: 10.2210/pdb6yi2/pdb
• NMR Information: BMRB: 50218
• Descriptor: DNA helicase (1 entity in total)
• Functional Keywords: dna-repair, tudor, uvrd, tcr, protein binding
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 8452.63

Authors

Kawale, A.A.,Burmann, B.B. (deposition date: 2020-03-31, release date: 2020-10-21, Last modification date: 2024-06-19)

Primary citation

Kawale, A.A.,Burmann, B.M.
UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.
Commun Biol, 3:607-607, 2020

PubMed Abstract: All living organisms have to cope with the constant threat of genome damage by UV light and other toxic reagents. To maintain the integrity of their genomes, organisms developed a variety of DNA repair pathways. One of these, the Transcription Coupled DNA-Repair (TCR) pathway, is triggered by stalled RNA Polymerase (RNAP) complexes at DNA damage sites on actively transcribed genes. A recently elucidated bacterial TCR pathway employs the UvrD helicase pulling back stalled RNAP complexes from the damage, stimulating recruitment of the DNA-repair machinery. However, structural and functional aspects of UvrD's interaction with RNA Polymerase remain elusive. Here we used advanced solution NMR spectroscopy to investigate UvrD's role within the TCR, identifying that the carboxy-terminal region of the UvrD helicase facilitates RNAP interactions by adopting a Tudor-domain like fold. Subsequently, we functionally analyzed this domain, identifying it as a crucial component for the UvrD-RNAP interaction besides having nucleic-acid affinity.

PubMed: 33097771
DOI: 10.1038/s42003-020-01332-2

Experimental method

SOLUTION NMR