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Open access
Nature Communications, volume 13, issue 1, publication number 3526

Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase

Fraser Alec 1
Sokolova Maria L 1, 2
Drobysheva Arina V 2
Gordeeva Julia V 2
Borukhov S. 3
Jumper John M. 4
Severinov Konstantin 2, 5, 6
Leiman Petr G. 1
1
 
Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, USA
3
 
Department of Cell Biology and Neuroscience, Rowan University School of Osteopathic Medicine at Stratford, Stratford, USA
4
 
DeepMind Technologies Limited, London, UK
6
 
Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Piscataway, USA
Publication typeJournal Article
Publication date2022-06-20
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor16.6
ISSN20411723
General Chemistry
General Biochemistry, Genetics and Molecular Biology
Multidisciplinary
General Physics and Astronomy
Abstract
Recognition of promoters in bacterial RNA polymerases (RNAPs) is controlled by sigma subunits. The key sequence motif recognized by the sigma, the −10 promoter element, is located in the non-template strand of the double-stranded DNA molecule ~10 nucleotides upstream of the transcription start site. Here, we explain the mechanism by which the phage AR9 non-virion RNAP (nvRNAP), a bacterial RNAP homolog, recognizes the −10 element of its deoxyuridine-containing promoter in the template strand. The AR9 sigma-like subunit, the nvRNAP enzyme core, and the template strand together form two nucleotide base-accepting pockets whose shapes dictate the requirement for the conserved deoxyuridines. A single amino acid substitution in the AR9 sigma-like subunit allows one of these pockets to accept a thymine thus expanding the promoter consensus. Our work demonstrates the extent to which viruses can evolve host-derived multisubunit enzymes to make transcription of their own genes independent of the host. Promoter recognition is a critical step in the initiation of transcription of DNA to RNA. Here, the authors describe a novel mechanism by which a phage-encoded RNA polymerase recognizes viral promoters containing deoxyuridines instead of thymidines.

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Fraser A. et al. Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase // Nature Communications. 2022. Vol. 13. No. 1. 3526
GOST all authors (up to 50) Copy
Fraser A., Sokolova M. L., Drobysheva A. V., Gordeeva J. V., Borukhov S., Jumper J. M., Severinov K., Leiman P. G. Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase // Nature Communications. 2022. Vol. 13. No. 1. 3526
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TY - JOUR
DO - 10.1038/s41467-022-31214-6
UR - https://doi.org/10.1038%2Fs41467-022-31214-6
TI - Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase
T2 - Nature Communications
AU - Fraser, Alec
AU - Sokolova, Maria L
AU - Drobysheva, Arina V
AU - Gordeeva, Julia V
AU - Borukhov, S.
AU - Jumper, John M.
AU - Severinov, Konstantin
AU - Leiman, Petr G.
PY - 2022
DA - 2022/06/20 00:00:00
PB - Springer Nature
IS - 1
VL - 13
SN - 2041-1723
ER -
BibTex
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BibTex Copy
@article{2022_Fraser,
author = {Alec Fraser and Maria L Sokolova and Arina V Drobysheva and Julia V Gordeeva and S. Borukhov and John M. Jumper and Konstantin Severinov and Petr G. Leiman},
title = {Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase},
journal = {Nature Communications},
year = {2022},
volume = {13},
publisher = {Springer Nature},
month = {jun},
url = {https://doi.org/10.1038%2Fs41467-022-31214-6},
number = {1},
doi = {10.1038/s41467-022-31214-6}
}
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