ArticlePloS one2011
Catalytic and non-catalytic roles for the mono-ADP-ribosyltransferase Arr in the mycobacterial DNA damage response.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Genomic insights into antibiotic resistance and mobilome of lactic acid bacteria and bifidobacteria.Life science alliance · 2023Article
- Deletion of rifampicin-inactivating mono-ADP-ribosyl transferase gene ofCurrent research in microbial sciences · 2022Article
- Kanglemycin A Can Overcome Rifamycin Resistance Caused by ADP-Ribosylation by Arr Protein.Antimicrobial agents and chemotherapy · 2021Article
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Species-Specific Interactions of Arr with RplK Mediate Stringent Response in Bacteria.Journal of bacteriology · 2018Article
- Rv0004 is a new essential member of the mycobacterial DNA replication machinery.PLoS genetics · 2017Article
- ADP-ribosylation: new facets of an ancient modification.The FEBS journal · 2017Review
- Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor.The Journal of biological chemistry · 2016Article
- Article
- Genomics-guided analysis of NAD recycling yields functional elucidation of COG1058 as a new family of pyrophosphatases.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Recent evidence indicates that the mycobacterial response to DNA double strand breaks (DSBs) differs substantially from previously characterized bacteria. These differences include the use of three DSB repair pathways (HR, NHEJ, SSA), and the CarD pathway, which integrates DNA damage with transcription. Here we identify a role for the mono-ADP-ribosyltransferase Arr in the mycobacterial DNA damage response. Arr is transcriptionally induced following DNA damage and cellular stress. Although Arr is not required for induction of a core set of DNA repair genes, Arr is necessary for suppression of a set of ribosomal protein genes and rRNA during DNA damage, placing Arr in a similar pathway as CarD. Surprisingly, the catalytic activity of Arr is not required for this function, as catalytically inactive Arr was still able to suppress ribosomal protein and rRNA expression during DNA damage. In contrast, Arr substrate binding and catalytic activities were required for regulation of a small subset of other DNA damage responsive genes, indicating that Arr has both catalytic and noncatalytic roles in the DNA damage response. Our findings establish an endogenous cellular function for a mono-ADP-ribosyltransferase apart from its role in mediating Rifampin resistance.
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Registered trials
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