The intrinsic ATPase activity of <i>Mycobacterium tuberculosis</i> UvrC is crucial for its damage‐specific DNA incision function

Thakur, Manoj; Agarwal, Ankit; Muniyappa, K.

doi:10.1111/febs.15465

Cited by 11 publications

(3 citation statements)

References 67 publications

(148 reference statements)

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“…2 and with the prokaryotic pattern of dual incisions 7 nucleotides 5' and 3-4 nucleotides 3' to the Pyr-Pyr. A different set of incision sites were described for M. tuberculosis repair, likely due to the use of indirect evidence for the 3' incision site and the absence of UvrA and UvrB in repair reactions in appropriate amounts (19).…”

Section: Smegmatis Removes Cyclobutane Pyrimidine Dimers From the mentioning

confidence: 99%

“…Against this background, then, it was rather unexpected when it was recently reported that in Mycobacterium tuberculosis (which possess the UvrA, B, and C homologs), the UvrC protein alone was capable of making dual incisions bracketing a bulky adduct 15 nucleotides 3' and 9 nucleotides 5' flanking the damage to generate a 25-mer, and it was concluded that dual incisions made by uvrC in M. tuberculosis are analogous to those made by its orthologs in yeast and humans (19). In light of this report, we decided to investigate dual incisions in Mycobacteria using M. smegmatis as representative of the genus.…”

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confidence: 99%

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Mycobacteria excise DNA damage in 12- or 13-nucleotide-long oligomers by prokaryotic-type dual incisions and performs transcription-coupled repair

Selby

Lindsey-Boltz

Yang

et al. 2020

Journal of Biological Chemistry

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In nucleotide excision repair, bulky DNA lesions such as UV-induced cyclobutane pyrimidine dimers (CPDs) are removed from the genome by concerted dual incisions bracketing the lesion, followed by gap filling and ligation. So far, two dual incision patterns have been discovered: prokaryotic type which removes the damage in 11-13 nucleotide-long oligomers and eukaryotic type which removes the damage in 24-32 nucleotide-long oligomers. However, a recent study reported that the UvrC protein of Mycobacterium tuberculosis removes damage in a manner analogous to yeast and humans in a 25-mer oligonucleotide arising from incisions at 15 nucleotides from the 3’ end and 9 nucleotides from the 5’ end flanking the damage. To test this model, we used the in vivo excision assay and the XR-seq genome-wide repair mapping method developed in our lab to determine the repair pattern and genome-wide repair map of M. smegmatis. We find that M. smegmatis, which possesses homologues of the E. coliuvrA, B, and C genes, removes CPDs from the genome in a manner identical to the prokaryotic pattern by incising 7 nucleotides 5’ and 3 or 4 nucleotides 3’ to the photoproduct, and performs transcription-coupled repair in a manner similar to E. coli.

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Section: Smegmatis Removes Cyclobutane Pyrimidine Dimers From the mentioning

confidence: 99%

mentioning

confidence: 99%

Mycobacteria excise DNA damage in 12- or 13-nucleotide-long oligomers by prokaryotic-type dual incisions and performs transcription-coupled repair

Selby

Lindsey-Boltz

Yang

et al. 2020

Journal of Biological Chemistry

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“…UvrC is an enzyme possessing a dual endonuclease activity catalyzed by two independent endonuclease domains: one located at its N-terminus that is responsible for the 3′ incision and another located at its C-terminus that is in charge of the 5′ incision ( 1–3 , 23–26 ). Mycobacterium tuberculosis UvrC (MtUvrC) has additionally been shown to possess an intrinsic DNA-independent ATPase activity ( 27 ). Crystal structures of the two catalytic domains of Thermatoga maritima UvrC (TmUvrC) have been determined.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER

Seck

Bonis

Stelter

et al. 2023

Nucleic Acids Research

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Bacterial nucleotide excision repair (NER), mediated by the UvrA, UvrB and UvrC proteins is a multistep, ATP-dependent process, that is responsible for the removal of a very wide range of chemically and structurally diverse DNA lesions. DNA damage removal is performed by UvrC, an enzyme possessing a dual endonuclease activity, capable of incising the DNA on either side of the damaged site to release a short single-stranded DNA fragment containing the lesion. Using biochemical and biophysical approaches, we have probed the oligomeric state, UvrB- and DNA-binding abilities and incision activities of wild-type and mutant constructs of UvrC from the radiation resistant bacterium, Deinococcus radiodurans. Moreover, by combining the power of new structure prediction algorithms and experimental crystallographic data, we have assembled the first model of a complete UvrC, revealing several unexpected structural motifs and in particular, a central inactive RNase H domain acting as a platform for the surrounding domains. In this configuration, UvrC is maintained in a ‘closed’ inactive state that needs to undergo a major rearrangement to adopt an ‘open’ active state capable of performing the dual incision reaction. Taken together, this study provides important insight into the mechanism of recruitment and activation of UvrC during NER.

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Global genome and transcription-coupled nucleotide excision repair pathway in prokaryotes

Thakur,

Muniyappa

2023

J Biosci

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The intrinsic ATPase activity of Mycobacterium tuberculosis UvrC is crucial for its damage‐specific DNA incision function

Cited by 11 publications

References 67 publications

Mycobacteria excise DNA damage in 12- or 13-nucleotide-long oligomers by prokaryotic-type dual incisions and performs transcription-coupled repair

Mycobacteria excise DNA damage in 12- or 13-nucleotide-long oligomers by prokaryotic-type dual incisions and performs transcription-coupled repair

Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER

Global genome and transcription-coupled nucleotide excision repair pathway in prokaryotes

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