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Molecular basis for the initiation of DNA primer synthesis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F22%3A00127814" target="_blank" >RIV/00216224:14310/22:00127814 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.nature.com/articles/s41586-022-04695-0" target="_blank" >https://www.nature.com/articles/s41586-022-04695-0</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41586-022-04695-0" target="_blank" >10.1038/s41586-022-04695-0</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Molecular basis for the initiation of DNA primer synthesis

  • Original language description

    During the initiation of DNA replication, oligonucleotide primers are synthesized de novo by primases and are subsequently extended by replicative polymerases to complete genome duplication. The primase-polymerase (Prim-Pol) superfamily is a diverse grouping of primases, which includes replicative primases and CRISPR-associated primase-polymerases (CAPPs) involved in adaptive immunity(1-3). Although much is known about the activities of these enzymes, the precise mechanism used by primases to initiate primer synthesis has not been elucidated. Here we identify the molecular bases for the initiation of primer synthesis by CAPP and show that this mechanism is also conserved in replicative primases. The crystal structure of a primer initiation complex reveals how the incoming nucleotides are positioned within the active site, adjacent to metal cofactors and paired to the templating single-stranded DNA strand, before synthesis of the first phosphodiester bond. Furthermore, the structure of a Prim-Pol complex with double-stranded DNA shows how the enzyme subsequently extends primers in a processive polymerase mode. The structural and mechanistic studies presented here establish how Prim-Pol proteins instigate primer synthesis, revealing the requisite molecular determinants for primer synthesis within the catalytic domain. This work also establishes that the catalytic domain of Prim-Pol enzymes, including replicative primases, is sufficient to catalyse primer formation.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nature

  • ISSN

    0028-0836

  • e-ISSN

    1476-4687

  • Volume of the periodical

    605

  • Issue of the periodical within the volume

    7911

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    7

  • Pages from-to

    767-773

  • UT code for WoS article

    000790783300002

  • EID of the result in the Scopus database

    2-s2.0-85129589357