ArticleNature structural & molecular biology2009
Nucleic acid polymerases use a general acid for nucleotidyl transfer.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.
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Who cites it
133 citing papers in PubMed, 219 citations in OpenAlex.
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- Dynamic diversity of SARS-CoV-2 genetic mutations in a lung transplantation patient with persistent COVID-19.Nature communications · 2024Article
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- Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN domain.Molecular cell · 2023Article
- Trivalent rare earth metal cofactors confer rapid NP-DNA polymerase activity.Science (New York, N.Y.) · 2023Article
- Molecular Anatomy of the Class I Ligase Ribozyme for Elucidation of the Activity-Generating Unit.Biology · 2023Article
- Kill or corrupt: Mechanisms of action and drug-resistance of nucleotide analogues against SARS-CoV-2.Antiviral research · 2023Review
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- Mobile genetic element-encoded putative DNA primases composed of A-family polymerase-SSB pairs.Frontiers in molecular biosciences · 2023Article
- Acquisition of Dual Ribozyme-Functions in Nonfunctional Short Hairpin RNAs through Kissing-Loop Interactions.Life (Basel, Switzerland) · 2022Article
- Mechanism of reaction of RNA-dependent RNA polymerase from SARS-CoV-2.Chem catalysis · 2022Article
- RdRp (RNA-dependent RNA polymerase): A key target providing anti-virals for the management of various viral diseases.Journal of molecular structure · 2022Review
- Two-Metal-Ion Catalysis: Inhibition of DNA Polymerase Activity by a Third Divalent Metal Ion.Frontiers in molecular biosciences · 2022Review
- Conserved Trigger Loop Histidine of RNA Polymerase II Functions as a Positional Catalyst Primarily through Steric Effects.Biochemistry · 2021Article
73 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Nucleic acid polymerases catalyze the formation of DNA or RNA from nucleoside-triphosphate precursors. Amino acid residues in the active site of polymerases are thought to contribute only indirectly to catalysis by serving as ligands for the two divalent cations that are required for activity or substrate binding. Two proton-transfer reactions are necessary for polymerase-catalyzed nucleotidyl transfer: deprotonation of the 3'-hydroxyl nucleophile and protonation of the pyrophosphate leaving group. Using model enzymes representing all four classes of nucleic acid polymerases, we show that the proton donor to pyrophosphate is an active-site amino acid residue. The use of general acid catalysis by polymerases extends the mechanism of nucleotidyl transfer beyond that of the well-established two-metal-ion mechanism. The existence of an active-site residue that regulates polymerase catalysis may permit manipulation of viral polymerase replication speed and/or fidelity for virus attenuation and vaccine development.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.