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of 33
pro vyhledávání: '"Cyril M. Sanders"'
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Replicative hexameric helicases are fundamental components of replisomes. Here the authors resolve a cryo-EM structure of the E1 helicase from papillomavirus bound to a DNA replication fork, providing insights into the mechanism of DNA unwinding by t
Externí odkaz:
https://doaj.org/article/32ab17c170964352825d558a35b79273
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications
Nature Communications
Hexameric helicases are motor proteins that unwind double-stranded DNA (dsDNA) during DNA replication but how they are optimised for strand separation is unclear. Here we present the cryo-EM structure of the full-length E1 helicase from papillomaviru
Publikováno v:
Nucleic Acids Research
Pif1 is a multifunctional helicase and DNA processing enzyme that has roles in genome stability. The enzyme is conserved in eukaryotes and also found in some prokaryotes. The functions of human PIF1 (hPIF1) are also critical for survival of certain t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5bc47c61539a3122f41a16d84005c99
https://eprints.whiterose.ac.uk/142114/1/gkz028.pdf
https://eprints.whiterose.ac.uk/142114/1/gkz028.pdf
Publikováno v:
Nucleic Acids Research
Bacteriophage T5 has a 120 kb double-stranded linear DNA genome encoding most of the genes required for its own replication. This lytic bacteriophage has a burst size of ∼500 new phage particles per infected cell, demonstrating that it is able to t
Autor:
Saba, Dehghani-Tafti, Cyril M, Sanders
Publikováno v:
Nucleic Acids Research
UPF1 is a conserved helicase required for nonsense-mediated decay (NMD) regulating mRNA stability in the cytoplasm. Human UPF1 (hUPF1) is also needed for nuclear DNA replication. While loss of NMD is tolerated, loss of hUPF1 induces a DNA damage resp
Autor:
Cyril M. Sanders
Publikováno v:
Biochemical Journal. 430:119-128
Pif1 proteins are helicases that in yeast are implicated in the maintenance of genome stability. One activity of Saccharomyces cerevisiae Pif1 is to stabilize DNA sequences that could otherwise form deleterious G4 (G-quadruplex) structures by acting
Autor:
Cyril M. Sanders
Publikováno v:
Nucleic Acids Research
The papillomavirus replication protein E1 assembles on the viral origin of replication (ori) as a series of complexes. It has been proposed that the ori DNA is first melted by a head-to-tail double trimer of E1 that evolves into two hexamers that enc
Autor:
Dmytro Sizov, Oleg Kovalevskiy, Michail N. Isupov, Alfred A. Antson, Andrey Lebedev, Cyril M. Sanders
Publikováno v:
Nucleic Acids Research
Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first
Autor:
Alfred A. Antson, Philippa R. Seavers, Dmytro Sizov, Miguel Ortiz-Lombardía, Cyril M. Sanders
Publikováno v:
Nucleic Acids Research
Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characteriz
Autor:
Yuriy, Chaban, Jonathan A, Stead, Ksenia, Ryzhenkova, Fiona, Whelan, Ekaterina P, Lamber, Alfred, Antson, Cyril M, Sanders, Elena V, Orlova
Publikováno v:
Nucleic Acids Research
Hexameric helicases are processive DNA unwinding machines but how they engage with a replication fork during unwinding is unknown. Using electron microscopy and single particle analysis we determined structures of the intact hexameric helicase E1 fro