The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics

Autor: Diana A. Llerena Schiffmacher, Shun-Hsiao Lee, Katarzyna W. Kliza, Arjan F. Theil, Masaki Akita, Angela Helfricht, Karel Bezstarosti, Camila Gonzalo-Hansen, Haico van Attikum, Matty Verlaan-de Vries, Alfred C. O. Vertegaal, Jan H. J. Hoeijmakers, Jurgen A. Marteijn, Hannes Lans, Jeroen A. A. Demmers, Michiel Vermeulen, Titia K. Sixma, Tomoo Ogi, Wim Vermeulen, Alex Pines

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)

Abstract Transcription-blocking DNA lesions are specifically targeted by transcription-coupled nucleotide excision repair (TC-NER), which removes a broad spectrum of DNA lesions to preserve transcriptional output and thereby cellular homeostasis to c

Externí odkaz: https://doaj.org/article/ae22f3558ad948a0bf15ffe295f5314c

Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity

Autor: Robbert Q. Kim, Paul P. Geurink, Monique P. C. Mulder, Alexander Fish, Reggy Ekkebus, Farid El Oualid, Willem J. van Dijk, Duco van Dalen, Huib Ovaa, Hugo van Ingen, Titia K. Sixma

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)

Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a

Externí odkaz: https://doaj.org/article/822bd4cb8eb04f3199afc82488ed53d3

Unexpected moves

Autor: Susanne R Bruekner, Wietske Pieters, Alexander Fish, A Manuel Liaci, Serge Scheffers, Emily Rayner, Daphne Kaldenbach, Lisa Drost, Marleen Dekker, Sandrine van Hees-Stuivenberg, Elly Delzenne-Goette, Charlotte de Konink, Hellen Houlleberghs, Hendrikus Jan Dubbink, Abeer AlSaegh, Niels de Wind, Friedrich Förster, Hein te Riele, Titia K Sixma

Publikováno v: Nucleic Acids Research, 51(3), 1173-1188. Oxford University Press
Bruekner, S R, Pieters, W, Fish, A, Liaci, A M, Scheffers, S, Rayner, E, Kaldenbach, D, Drost, L, Dekker, M, van Hees-Stuivenberg, S, Delzenne-Goette, E, de Konink, C, Houlleberghs, H, Dubbink, H J, Alsaegh, A, de Wind, N, Förster, F, te Riele, H & Sixma, T K 2023, ' Unexpected moves : a conformational change in MutSα enables high-affinity DNA mismatch binding ', Nucleic Acids Research, vol. 51, no. 3, pp. 1173-1188 . https://doi.org/10.1093/nar/gkad015

The DNA mismatch repair protein MutSα recognizes wrongly incorporated DNA bases and initiates their correction during DNA replication. Dysfunctions in mismatch repair lead to a predisposition to cancer. Here, we study the homozygous mutation V63E in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b261243e65c36c88dc6a5fefdea17ff9
https://doi.org/10.1093/nar/gkad015

BAP1/ASXL1 recruitment and activation for H2A deubiquitination

Autor: Danny D. Sahtoe, Willem J. van Dijk, Reggy Ekkebus, Huib Ovaa, Titia K. Sixma

Publikováno v: Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)

The tumor suppressor BAP1 is activated by ASXL1 to deubiquitinate mono-ubiquitinated H2A at K119 in Polycomb gene repression. Here, the authors show how BAP1’s C-terminal extension auto-recruits it to nucleosomes, where the DEUBAD domain of ASXL1 i

Externí odkaz: https://doaj.org/article/0ea8dc04cd7544a2834c03123e450572

Mitoxantrone stacking does not define the active or inactive state of USP15 catalytic domain

Autor: Anu Priyanka, Dominic Tisi, Titia K. Sixma

Publikováno v: Journal of Structural Biology. 214:107862

Ubiquitin specific protease USP15 is a deubiquitinating enzyme reported to regulate several biological and cellular processes, including TGF-β signaling, regulation of immune response, neuro-inflammation and mRNA splicing. Here we study the USP15 D1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f73bb72dbe88c06a71ee25da34958a9
https://doi.org/10.1016/j.jsb.2022.107862