Recent advances in understanding bacterial and archaeoeukaryotic primases

dc.accessRightsAnonymous*
dc.audienceScienceen_US
dc.contributor.authorLipps, Georg
dc.date.accessioned2020-12-17T05:30:12Z
dc.date.available2020-12-17T05:30:12Z
dc.date.issued2019-12
dc.description.abstractDNA replication in all forms of life relies upon the initiation of synthesis on a single strand template by formation of a short oligonucleotide primer, which is subsequently elongated by DNA polymerases. Two structurally distinct classes of enzymes have evolved to perform this function, namely the bacterial DnaG-type primases and the Archaeal and Eukaryotic primases (AEP). Structural and mechanistic insights have provided a clear understanding of the role of the different domains of these enzymes in the context of the replisome and recent work sheds light upon primase-substrate interactions. We herein review the emerging picture of the primase mechanism on the basis of the structural knowledge obtained to date and propose future directions of this essential aspect of DNA replication.en_US
dc.identifier.doihttps://doi.org/10.1016/j.sbi.2019.08.004
dc.identifier.issn1879-033X
dc.identifier.issn0959-440X
dc.identifier.urihttps://irf.fhnw.ch/handle/11654/31880
dc.identifier.urihttps://doi.org/10.26041/fhnw-3563
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofCurrent Opinion in Structural Biologyen_US
dc.subjectreplication primaseen_US
dc.titleRecent advances in understanding bacterial and archaeoeukaryotic primasesen_US
dc.type01A - Beitrag in wissenschaftlicher Zeitschrift
dc.volume59en_US
dspace.entity.typePublication
fhnw.InventedHereYesen_US
fhnw.IsStudentsWorknoen_US
fhnw.PublishedSwitzerlandNoen_US
fhnw.ReviewTypeAnonymous ex ante peer review of a complete publicationen_US
fhnw.affiliation.hochschuleHochschule für Life Sciencesde_CH
fhnw.affiliation.institutInstitut für Chemie und Bioanalytikde_CH
fhnw.pagination159-167en_US
fhnw.publicationOnlineJaen_US
fhnw.publicationStatePublisheden_US
relation.isAuthorOfPublication30d5ac4a-5f57-468d-95b9-695fcc98d1bd
relation.isAuthorOfPublication.latestForDiscovery30d5ac4a-5f57-468d-95b9-695fcc98d1bd
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