scholarly journals Proteomic Investigations Reveal a Role for RNA Processing Factor THRAP3 in the DNA Damage Response

2012 ◽  
Vol 46 (2) ◽  
pp. 212-225 ◽  
Author(s):  
Petra Beli ◽  
Natalia Lukashchuk ◽  
Sebastian A. Wagner ◽  
Brian T. Weinert ◽  
Jesper V. Olsen ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Processing Factor ◽  
Damage Response

scholarly journals The RNA Processing Factor Y14 Participates in DNA Damage Response and Repair

iScience ◽  
2019 ◽  
Vol 13 ◽  
pp. 402-415 ◽  
Author(s):  
Tzu-Wei Chuang ◽  
Chia-Chen Lu ◽  
Chun-Hao Su ◽  
Pei-Yu Wu ◽  
Sarasvathi Easwvaran ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Processing Factor ◽  
Damage Response

scholarly journals PARprolink: a photoaffinity probe for identifying poly(ADP-ribose)-binding proteins

2020 ◽  
Author(s):  
Morgan Dasovich ◽  
Morgan Q. Beckett ◽  
Scott Bailey ◽  
Shao-En Ong ◽  
Marc M. Greenberg ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Binding Proteins ◽  
Post Translational Modification ◽  
Mobility Shift ◽  
Binding Partners ◽  
Damage Response ◽  
Prostate Cancers ◽  
Electrophoretic Mobility Shift Assays

ABSTRACTPost-translational modification of proteins with poly(ADP-ribose) (PAR) is an important component of the DNA damage response. Four PAR synthesis inhibitors have recently been approved for the treatment of breast, ovarian, and prostate cancers. Despite its clinical significance, a molecular understanding of PAR function, including its binding partners, remains incomplete. In this work, we synthesize a PAR photoaffinity probe that captures and isolates endogenous PAR binders. Our method identified dozens of known PAR-binding proteins and hundreds of novel binders involved in DNA repair, RNA processing, and metabolism. PAR binding by eight candidates was confirmed using pull-down and/or electrophoretic mobility shift assays. Using PAR probes of defined lengths, we detected proteins that preferentially bind to 40-mer over 8-mer PAR, indicating that polymer length may regulate the outcome and timing of PAR signaling pathways. This investigation produces the first census of PAR-binding proteins, provides a proteome-wide view of length-selective PAR binding, and associates PAR binding with RNA metabolism and the formation of biomolecular condensates.

scholarly journals The RNA processing factors THRAP3 and BCLAF1 promote the DNA damage response through selective mRNA splicing and nuclear export

2017 ◽  
Vol 45 (22) ◽  
pp. 12816-12833 ◽  
Author(s):  
Jekaterina Vohhodina ◽  
Eliana M. Barros ◽  
Abigail L. Savage ◽  
Fabio G. Liberante ◽  
Lorenzo Manti ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Nuclear Export ◽  
Mrna Splicing ◽  
Damage Response ◽  
Processing Factors

scholarly journals The DNA damage response activates HPV16 late gene expression at the level of RNA processing

2018 ◽  
Vol 46 (10) ◽  
pp. 5029-5049 ◽  
Author(s):  
Kersti Nilsson ◽  
Chengjun Wu ◽  
Naoko Kajitani ◽  
Haoran Yu ◽  
Efthymios Tsimtsirakis ◽  
...  
Keyword(s):  
Gene Expression ◽  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Late Gene ◽  
Late Gene Expression ◽  
Damage Response

scholarly journals The Human Exonuclease-1 Interactome And Phosphorylation Sites

2019 ◽  
Author(s):  
Wassim Eid ◽  
Daniel Hess ◽  
Christiane König ◽  
Christian Gentili ◽  
Stefano Ferrari
Keyword(s):  
Mass Spectrometry ◽  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
List Type ◽  
Phosphorylation Sites ◽  
Interacting Proteins ◽  
Damage Response ◽  
Causative Agents ◽  
Exonuclease 1

ABSTRACTError-free repair of DNA double-strand break is orchestrated by homologous recombination (HR) pathways and requires the concerted action of several factors. Among these, EXO1 and DNA2/BLM execute extensive resection of DNA ends to produce 3’-overhangs, which are key intermediates for downstream steps of HR. To help shedding light on regulatory aspects of DNA repair pathways in which EXO1 participates, we set out to identify proteins interacting with EXO1. Affinity purification of EXO1 followed by Orbitrap mass spectrometry led to the identification of novel partners that are involved in RNA processing or that are the causative agents of rare X-linked disorders. Depletion of a selected subset of EXO1 interacting proteins led to reduction of the DNA damage response. Among those, we examined the RRP5-homologue and NFκB-interacting protein PDCD11/ALG-4, which has roles in apoptosis and is a putative driver gene in cutaneous T-cell lymphoma. We provide evidence that depletion of PDCD11 decreased the formation of γH2AX foci and the phosphorylation of DNA damage response signaling intermediates in response to camptothecin or bleomycin, resulting in increased cellular resistance to DNA damage. Furthermore, extensive coverage of EXO1 sequence (>85%) by mass spectrometry allowed conducting an in-depth analysis of its phosphorylation sites, with the identification of 26 residues that are differentially modified in untreated conditions or upon induction of DNA damage.As a whole, these results provide the basis for future in-depth studies on novel roles of EXO1 in genome stability and indicate targets for pharmacological inhibition of pathways of cancer development.HIGHLIGHTSProteome-wide analysis of Exonuclease-1 (EXO1) interacting proteins revealed novel partners involved in RNA processing or that are the causative agents of rare X-linked disorders.We provide evidence for a role of PDCD11 in the DNA Damage Response.We conducted a comprehensive identification of EXO1 phosphorylation sites.

Maintenance of genome stability: the unifying role of interconnections between the DNA damage response and RNA-processing pathways

2018 ◽  
Vol 64 (5) ◽  
pp. 971-983 ◽  
Author(s):  
B. Mikolaskova ◽  
M. Jurcik ◽  
I. Cipakova ◽  
M. Kretova ◽  
M. Chovanec ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Processing ◽  
Genome Stability ◽  
Damage Response ◽  
Processing Pathways
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