ArticleBiochemistry2009
DNA recognition by the DNA primase of bacteriophage T7: a structure-function study of the zinc-binding domain.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- The plant organellar primase-helicase directs template recognition and primosome assembly via its zinc finger domain.BMC plant biology · 2023Article
- Relations between Structure and Zn(II) Binding Affinity Shed Light on the Mechanisms of Rad50 Hook Domain Functioning and Its Phosphorylation.International journal of molecular sciences · 2022Article
- DnaG Primase-A Target for the Development of Novel Antibacterial Agents.Antibiotics (Basel, Switzerland) · 2018Review
- Modulation of RNA primer formation by Mn(II)-substituted T7 DNA primase.Scientific reports · 2017Article
- Optimal numbers of residues in linkers of DNA polymerase I, T7 primase and DNA polymerase IV.Scientific reports · 2016Article
- Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex.Biochemistry · 2014Article
- Zinc-binding domain of the bacteriophage T7 DNA primase modulates binding to the DNA template.The Journal of biological chemistry · 2012Article
- Characterization of a nucleotide kinase encoded by bacteriophage T7.The Journal of biological chemistry · 2012Article
- The roles of tryptophans in primer synthesis by the DNA primase of bacteriophage T7.The Journal of biological chemistry · 2012Article
- Gene 5.5 protein of bacteriophage T7 in complex with Escherichia coli nucleoid protein H-NS and transfer RNA masks transfer RNA priming in T7 DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Pyrovanadolysis, a pyrophosphorolysis-like reaction mediated by pyrovanadate, Mn2+, and DNA polymerase of bacteriophage T7.The Journal of biological chemistry · 2011Article
- Binding of Mn-deoxyribonucleoside triphosphates to the active site of the DNA polymerase of bacteriophage T7.Powder diffraction · 2011Article
- Communication between the zinc and nickel sites in dimeric HypA: metal recognition and pH sensing.Journal of the American Chemical Society · 2010Article
- Mechanism of sequence-specific template binding by the DNA primase of bacteriophage T7.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Synthesis of oligoribonucleotide primers for lagging-strand DNA synthesis in the DNA replication system of bacteriophage T7 is catalyzed by the primase domain of the gene 4 helicase-primase. The primase consists of a zinc-binding domain (ZBD) and an RNA polymerase (RPD) domain. The ZBD is responsible for recognition of a specific sequence in the ssDNA template whereas catalytic activity resides in the RPD. The ZBD contains a zinc ion coordinated with four cysteine residues. We have examined the ligation state of the zinc ion by X-ray absorption spectroscopy and biochemical analysis of genetically altered primases. The ZBD of primase engaged in catalysis exhibits considerable asymmetry in coordination to zinc, as evidenced by a gradual increase in electron density of the zinc together with elongation of the zinc-sulfur bonds. Both wild-type primase and primase reconstituted from purified ZBD and RPD have a similar electronic change in the level of the zinc ion as well as the configuration of the ZBD. Single amino acid replacements in the ZBD (H33A and C36S) result in the loss of both zinc binding and its structural integrity. Thus the zinc in the ZBD may act as a charge modulation indicator for the surrounding sulfur atoms necessary for recognition of specific DNA sequences.
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