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Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase
Ludovic Sauguet, Sebastian Klinge, Rajika Perera, Joseph Maman, Luca Pellegrini

Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase

Science & Mathematics Published 2010 Verification Pending

Overview & Synopsis

DNA synthesis during replication relies on RNA primers synthesised by the primase, a specialised DNA-dependent RNA polymerase that can initiate nucleic acid synthesis de novo. In archaeal and eukaryotic organisms, the primase is a heterodimeric enzyme resulting from the constitutive association of a small (PriS) and large (PriL) subunit. The ability of the primase to initiate synthesis of an RNA primer depends on a conserved Fe-S domain at the C-terminus of PriL (PriL-CTD). However, the critical role of the PriL-CTD in the catalytic mechanism of initiation is not understood.

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Document Information

Document Title Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase
Author / Organization Ludovic Sauguet, Sebastian Klinge, Rajika Perera, Joseph Maman, Luca Pellegrini
Subject & Discipline Multidisciplinary Academic Open Research
Categories Science & Mathematics
Publication Year 2010
License / Rights Open Access / Creative Commons
Resource Verification Listed PDF (Verification Pending)
Original Host Website HAL Open Science (hal.science)
File Format application/pdf (Portable Document Format)
Language EN
Catalog ID DOC-257593
Original Source Link Visit Source Page on hal.science »