ArticleMolecular and cellular biology2003
Deoxynucleotide triphosphate binding mode conserved in Y family DNA polymerases.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
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- Second-Shell Basic Residues Expand the Two-Metal-Ion Architecture of DNA and RNA Processing Enzymes.Structure (London, England : 1993) · 2018Article
- Kinetic and Structural Impact of Metal Ions and Genetic Variations on Human DNA Polymerase ι.The Journal of biological chemistry · 2016Article
- Biochemical analysis of six genetic variants of error-prone human DNA polymerase ι involved in translesion DNA synthesis.Chemical research in toxicology · 2014Article
- A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli.Nucleic acids research · 2013Article
- Essential role of Tip60-dependent recruitment of ribonucleotide reductase at DNA damage sites in DNA repair during G1 phase.Genes & development · 2010Article
- Eukaryotic translesion polymerases and their roles and regulation in DNA damage tolerance.Microbiology and molecular biology reviews : MMBR · 2009Review
- Article
- Accommodation of a 1S-(-)-benzo[c]phenanthrenyl-N6-dA adduct in the Y-family Dpo4 DNA polymerase active site: structural insights through molecular dynamics simulations.Chemical research in toxicology · 2005Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Although DNA polymerase eta (Pol eta) and other Y family polymerases differ in sequence and function from classical DNA polymerases, they all share a similar right-handed architecture with the palm, fingers, and thumb domains. Here, we examine the role in Saccharomyces cerevisiae Pol eta of three conserved residues, tyrosine 64, arginine 67, and lysine 279, which come into close contact with the triphosphate moiety of the incoming nucleotide, in nucleotide incorporation. We find that mutational alteration of these residues reduces the efficiency of correct nucleotide incorporation very considerably. The high degree of conservation of these residues among the various Y family DNA polymerases suggests that these residues are also crucial for nucleotide incorporation in the other members of the family. Furthermore, we note that tyrosine 64 and arginine 67 are functionally equivalent to the deoxynucleotide triphosphate binding residues arginine 518 and histidine 506 in T7 DNA polymerase, respectively.
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Registered trials
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.