ArticleJournal of bacteriology2010
Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- New option: targeting RNase J and RNase HI in the fight against multi-drug-resistant tuberculosis.Annals of medicine and surgery (2012) · 2024Article
- The C-Terminal Acid Phosphatase Module of the RNase HI Enzyme RnhC Controls Rifampin Sensitivity and Light-Dependent Colony Pigmentation of Mycobacterium smegmatis.Journal of bacteriology · 2023Article
- RNase HI Depletion Strongly Potentiates Cell Killing by Rifampicin in Mycobacteria.Antimicrobial agents and chemotherapy · 2022Article
- Biosynthesis of Tetrapyrrole Cofactors by Bacterial Community Inhabiting Porphyrine-Containing Shale Rock (Fore-Sudetic Monocline).Molecules (Basel, Switzerland) · 2021Article
- Functional Disassociation Between the Protein Domains of MSMEG_4305 ofFrontiers in microbiology · 2020Article
- The Clash of Macromolecular Titans: Replication-Transcription Conflicts in Bacteria.Annual review of microbiology · 2018Review
- DNA Replication in Mycobacterium tuberculosis.Microbiology spectrum · 2017Review
- Division of labor among Mycobacterium smegmatis RNase H enzymes: RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase.Nucleic acids research · 2017Article
- Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016Review
- Use of siRNA molecular beacons to detect and attenuate mycobacterial infection in macrophages.World journal of experimental medicine · 2015Review
- Biochemical Characterization of Mycobacterium smegmatis RnhC (MSMEG_4305), a Bifunctional Enzyme Composed of Autonomous N-Terminal Type I RNase H and C-Terminal Acid Phosphatase Domains.Journal of bacteriology · 2015Article
- Article
- The deletion of rnhB in Mycobacterium smegmatis does not affect the level of RNase HII substrates or influence genome stability.PloS one · 2015Article
- Mycobacterium smegmatis DinB2 misincorporates deoxyribonucleotides and ribonucleotides during templated synthesis and lesion bypass.Nucleic acids research · 2014Article
- MS_RHII-RSD, a dual-function RNase HII-(p)ppGpp synthetase from Mycobacterium smegmatis.Journal of bacteriology · 2012Article
- A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeon Halobacterium sp. NRC-1.FEBS open bio · 2012Article
- Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis.Scientific reports · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with alpha-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. The full-length protein was shown to have additional CobC activity. The crystal structure of the MBP-Rv2228c/N fusion protein was solved by molecular replacement and refined at 2.25-A resolution (R = 0.182; R(free) = 0.238). The protein is monomeric in solution but associates in the crystal to form a dimer. The Rv2228c/N domain has the classic RNase H fold and catalytic machinery but lacks several surface features that play important roles in the cleavage of RNA/DNA hybrids by other RNases H. The absence of either the basic protrusion of some RNases H or the hybrid binding domain of others appears to be compensated by the C-terminal CobC domain in full-length Rv2228c. The double-stranded-RNase activity of Rv2228c/N contrasts with classical RNases H and is attributed to the absence in Rv2228c/N of a key phosphate binding pocket.
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