The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.

Autor: Jirapas Jongjitwimol, Min Feng, Lihong Zhou, Oliver Wilkinson, Lauren Small, Robert Baldock, Deborah L Taylor, Duncan Smith, Lucas D Bowler, Simon J Morley, Felicity Z Watts

Publikováno v: PLoS ONE, Vol 9, Iss 5, p e94182 (2014)

SUMO is a small post-translational modifier, that is attached to lysine residues in target proteins. It acts by altering protein-protein interactions, protein localisation and protein activity. SUMO chains can also act as substrates for ubiquitinatio

Externí odkaz: https://doaj.org/article/92214a3ec7214f9bb813caae917cf735

SUMO chain formation is required for response to replication arrest in S. pombe.

Autor: Andrew Skilton, Jenny C Y Ho, Brenda Mercer, Emily Outwin, Felicity Z Watts

Publikováno v: PLoS ONE, Vol 4, Iss 8, p e6750 (2009)

SUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold presen

Externí odkaz: https://doaj.org/article/6c36f3bfe97a44dd988e0eb5d4fb4ed4

Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 to control the G1 DNA damage checkpoint

Autor: Matthew Day, Felicity Z. Watts, Laurence H. Pearl, Antony W. Oliver, Nicolas Bigot, Robert A Baldock

Publikováno v: Bigot, N, Day, M, Baldock, R A, Watts, F Z, Oliver, A W & Pearl, L H 2019, ' Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 to control the G1 DNA damage checkpoint ', eLife, vol. 8 . https://doi.org/10.7554/eLife.44353
eLife, Vol 8 (2019)

SUMMARYCoordination of the cellular response to DNA damage is organised by multi-domain ‘scaffold’ proteins, including 53BP1 and TOPBP1, which recognise post-translational modifications such as phosphorylation, methylation and ubiquitylation on o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c44247bc34b96d3e5043de507df52cd2

Drosha drives the formation of DNA:RNA hybrids around DNA break sites to facilitate DNA repair

Autor: Aldo S. Bader, Wei-Ting Lu, Michal Malewicz, Ania Wilczynska, Robert A Baldock, Ewan M. Smith, Martin Bushell, Ben R Hawley, George Skalka, Felicity Z. Watts

Publikováno v: Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)

The error-free and efficient repair of DNA double-stranded breaks (DSBs) is extremely important for cell survival. RNA has been implicated in the resolution of DNA damage but the mechanism remains poorly understood. Here, we show that miRNA biogenesi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9fe86a8f722e28e73e39fe13472c257
https://eprints.glos.ac.uk/9779/8/9779-Baldock-(2018)-Drosha-drives-the-formation-of-DNARNA-hybrids.pdf

Repair of DNA double-strand breaks in heterochromatin

Autor: Felicity Z. Watts

Publikováno v: Biomolecules, Vol 6, Iss 4, p 47 (2016)
Biomolecules

DNA double-strand breaks (DSBs) are among the most damaging lesions in DNA, since, if not identified and repaired, they can lead to insertions, deletions or chromosomal rearrangements. DSBs can be in the form of simple or complex breaks, and may be r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4918f7152ea8685177da227767c4e98