Blar i forfatter "Moe, Elin"
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Advances in the expression and purification of human PARP1: A user-friendly protocol
Conceição, Carlota J.F.; Salgueiro, Bruno A.; Ribeiro, Paulo A.; Raposo, Maria; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-07-05)The PARP1 (Poly (ADP-ribose) polymerase 1) enzyme is essential for single and double-strand break repair in humans. Alterations affecting PARP1 activity have severe consequences for human health and are associated with pathologies like cancer, and metabolic and neurodegenerative disorders. Here, we have developed a fast and easy procedure for the expression and purification of PARP1. Biologically ... -
Crystal structure of the DNA polymerase III β subunit (β-clamp) from the extremophile Deinococcus radiodurans
Niiranen, Laila; Lian, Kjersti; Johnson, Kenneth A; Moe, Elin (Journal article; Tidsskriftartikkel, 2015-02-27)Background: Deinococcus radiodurans is an extremely radiation and desiccation resistant bacterium which can tolerate radiation doses up to 5,000 Grays without losing viability. We are studying the role of DNA repair and replication proteins for this unusual phenotype by a structural biology approach. The DNA polymerase III β subunit (β-clamp) acts as a sliding clamp on DNA, promoting the binding ... -
A Decade of Biochemical and Structural Studies of the DNA Repair Machinery of Deinococcus radiodurans: Major Findings, Functional and Mechanistic Insight and Challenges
Timmins, Joanna; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2016-04-27)The Deinococcus radiodurans bacterium is extremely resistant to ionising radiation and desiccation and can withstand a 200-fold higher radiation dose than most other bacteria with no loss of viability. The mechanisms behind this extreme resistance are not fully understood, but it is clear that several factors contribute to this phenotype. Efficient scavenging of reactive oxygen species and repair ... -
Insights into the role of three Endonuclease III enzymes for oxidative stress resistance in the extremely radiation resistant bacterium Deinococcus radiodurans
Rollo, Filipe; Martins, Guilherme D.; Gouveia, André G.; Ithurbide, Solenne; Servant, Pascale; Romão, Célia V.; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-09-12)The extremely radiation and desiccation resistant bacterium Deinococcus radiodurans possesses three genes encoding Endonuclease III-like enzymes (DrEndoIII1, DrEndoIII2, DrEndoIII3). In vitro enzymatic activity measurements revealed that DrEndoIII2 is the main Endonuclease III in this organism, while DrEndoIII1 and 3 possess unusual and, so far, no detectable EndoIII activity, respectively. In ... -
Liposome Formulations for the Strategic Delivery of PARP1 Inhibitors: Development and Optimization
Conceição, Carlota J. F.; Moe, Elin; Ribeiro, Paulo A.; Raposo, Maria (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-05-11)first_pagesettingsOrder Article Reprints Open AccessArticle Liposome Formulations for the Strategic Delivery of PARP1 Inhibitors: Development and Optimization by Carlota J. F. Conceição 1,2ORCID,Elin Moe 3,4,Paulo A. Ribeiro 2ORCID andMaria Raposo 2,*ORCID 1 CEFITEC, Department of Physics, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516 Caparica, Portugal 2 Laboratory ... -
MutT from the fish pathogen Aliivibrio salmonicida is a cold active nucleotide pool sanitization enzyme with an unexpected high thermostability
Lian, Kjersti; Leiros, Hanna-Kirsti S.; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2015) -
Structural and biophysical analysis of interactions between cod and human uracil-DNA N-glycosylase (UNG) and UNG inhibitor (Ugi)
Assefa, Netsanet Gizaw; Niiranen, Laila; Johnson, Kenneth; Leiros, Hanna-Kirsti S.; Smalås, Arne O.; Willassen, Nils Peder; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2014-07-25)Uracil-DNA N-glycosylase from Atlantic cod (cUNG) shows cold-adapted features such as high catalytic efficiency, a low temperature optimum for activity and reduced thermal stability compared with its mesophilic homologue human UNG (hUNG). In order to understand the role of the enzyme–substrate interaction related to the cold-adapted properties, the structure of cUNG in complex with a bacteriophage ... -
Structure determination of uracil-DNA N-glycosylase from Deinococcus radiodurans in complex with DNA
Pedersen, Hege Lynum; Johnson, Kenneth; McVey, Colin; Leiros, Ingar; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2015-10-01) -
Structure/function studies of the NAD<sup>+</sup>-dependent DNA ligase from the poly-extremophile Deinococcus radiodurans reveal importance of the BRCT domain for DNA binding
Fernandes, Andreia; Williamson, Adele Kim; Matias, Pedro M.; Moe, Elin (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-09-15)Bacterial NAD<sup>+</sup>-dependent DNA ligases (LigAs) are enzymes involved in replication, recombination, and DNA-repair processes by catalyzing the formation of phosphodiester bonds in the backbone of DNA. These multidomain proteins exhibit four modular domains, that are highly conserved across species, with the BRCT (breast cancer type 1 C-terminus) domain on the C-terminus of the enzyme. In ... -
The three Endonuclease III variants of Deinococcus radiodurans possess distinct and complementary DNA repair activities
Sarre, Aili; Stelter, Meike; Rollo, Filipe; De Bonis, Salvatore; Seck, Anna; Hognon, Cecilia; Ravanat, Jean-Luc; Monari, Antonio; Dehez, Francois; Moe, Elin; Timmins, Joanna (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-03-28)Endonuclease III (EndoIII) is a bifunctional DNA glycosylase that removes oxidized pyrimidines from DNA. The genome of Deinococcus radiodurans encodes for an unusually high number of DNA glycosylases, including three EndoIII enzymes (drEndoIII1-3). Here, we compare the properties of these enzymes to those of their well-studied homologues from E. coli and human. Our biochemical and mutational data, ...