ReviewComputational and structural biotechnology journal2015
Structures to complement the archaeo-eukaryotic primases catalytic cycle description: What's next?
Review in Computational and structural biotechnology journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Article
- Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.The journal of physical chemistry. B · 2020Article
- Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.Frontiers in molecular biosciences · 2020Article
- Article
- Novel Families of Archaeo-Eukaryotic Primases Associated with Mobile Genetic Elements of Bacteria and Archaea.Journal of molecular biology · 2018Article
- TruePrime is a novel method for whole-genome amplification from single cells based on TthPrimPol.Nature communications · 2016Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA replication is a crucial stage in the transfer of genetic information from parent to daughter cells. This mechanism involves multiple proteins with one key player being the primase. Primases are single-stranded DNA dependent RNA polymerases. On the leading strand, they synthesize the primer once allowing DNA elongation while on the lagging strand primers are generated repeatedly (Okazaki fragments). Primases have the unique ability to create the first phosphodiester bond yielding a dinucleotide which is initially elongated by primases and then by DNA polymerases. Primase activity has been studied in the last decades but the detailed molecular steps explaining some unique features remain unclear. High-resolution structures of free and bound primases domains have brought significant insights in the understanding of the primase reaction cycle. Here, we give a short review of the structural work conducted in the field of archaeo-eukaryotic primases and we underline the missing "pictures" of the active forms of the enzyme which are of major interest. We organized our analysis with respect to the progression through the catalytic pathway.
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