ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair

Gracheva, Ekaterina; Chitale, Shalaka; Wilhelm, Thomas; Rapp, Alexander; Byrne, Jonathan; Stadler, Jens M.; Medina, Rebeca; Cardoso, M. Cristina; Richly, Holger

doi:10.1083/jcb.201506099

Cited by 38 publications

(73 citation statements)

References 55 publications

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“…For example, S. cerevisiae Zuo1 activates Pdr1, a transcription factor implicated in quorum sensing 27,49 . Human DnaJC2 functions as a chromatin modulator, affecting development and DNA repair 50,51 . Thus, via both on- and off-ribosome functions, Zuo1/DnaJC2 may play a more global regulatory role than we presently appreciate, coordinating protein synthesis and folding with other aspects of gene expression and cell physiology.…”

Section: Discussionmentioning

confidence: 99%

Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Lee

Sharma

Shrestha

et al. 2016

Nat Struct Mol Biol

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Ribosome-associated J protein-Hsp70 chaperones promote nascent polypeptide folding and normal translational fidelity. Though known to span the ribosome subunits, understanding of J protein Zuo1 function is limited. New structural and crosslinking data allow more precise positioning of Saccharomyces cerevisiae Zuo1 near the 60S polypeptide exit site, pointing to interactions with ribosomal protein eL31 and 25S rRNA helix 24. The junction between the 60S-interacting and subunit-spanning helices is a hinge, positioning Zuo1 on the 40S, yet accommodating subunit rotation. Interaction between C-terminus of Zuo1 and 40S occurs via 18S rRNA expansion segment 12 (ES12) of helix 44, which originates at the decoding site. Deletions in either ES12 or C-terminus of Zuo1 alter stop codon readthrough and −1 frameshifting. Our study offers insight into how this cotranslational chaperone system may monitor decoding site activity and nascent polypeptide transit, thereby coordinating protein translation and folding.

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Section: Discussionmentioning

confidence: 99%

Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Lee

Sharma

Shrestha

et al. 2016

Nat Struct Mol Biol

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“…A major signal at chromatin and its associated proteins are ubiquitylation events that are catalyzed by specific E3 ubiquitin ligases. Various E3 ligases have been identified in the global genomic branch of NER (GG-NER) [35,[37][38][39][40], which describes DNA repair at non transcribed regions of the genome (Information Box 1). Although, substrates of the DNA damage specific E3 ligases are known (Table 1), how ubiquitin signaling at the DNA damage site is orchestrated remains largely unknown.…”

Section: E3 Ubiquitin Ligases: Essential Regulators Of the Dna Damagementioning

confidence: 99%

“…Mono-ubiquitylation at histone H2A is catalyzed by DDB E3 ligase complexes during damage recognition and additionally by the RING-containing E3 ligase RNF8 at later stages of DNA repair [40] ( Table 1). The UV-RING1B complex, like its cousin PRC1, and the DDB-CUL4 B complex catalyze ubiquitylation of lysine 119 of histone H2A [35,41]. Still, not much is known about the substrate specificity of any of the E3 ligases involved in NER.…”

Section: E3 Ubiquitin Ligases: Essential Regulators Of the Dna Damagementioning

confidence: 99%

“…Both the UV-RING1B complex and PRC1 specifically ubiquitylate lysine 119 at histone H2A. ZRF1 shows a high affinity for the mono-ubiquitin residue at this particular amino acid [28,35]. In contrast, whether the DDB-CUL4A E3 ligase sets the ubiquitin mark at lysine 119 is arguable.…”

Section: Zrf1 Promotes On-site Remodeling Of E3 Ligase Complexes Durimentioning

confidence: 99%

“…Two recent studies propose that ZRF1 facilitates remodeling of multiprotein complexes, both at DNA damage sites during NER [35] and at gene regulatory elements during the transcriptional activation of Polycomb-repressed genes [36]. During NER, ZRF1 mediates the re-organization of E3 ligase complexes, thereby changing their substrate specificity and driving poly-ubiquitylation events.…”

Section: Introductionmentioning

confidence: 99%

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On‐site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation

Papadopoulou

Richly

2016

BioEssays

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In this review, we discuss a novel on-site remodeling function that is mediated by the H2A-ubiquitin binding protein ZRF1. ZRF1 facilitates the remodeling of multiprotein complexes at chromatin and lies at the heart of signaling processes that occur at DNA damage sites and during transcriptional activation. In nucleotide excision repair ZRF1 remodels E3 ubiquitin ligase complexes at the damage site. During embryonic stem cell differentiation, it contributes to retinoic acid-mediated gene activation by altering the subunit composition of the Mediator complex. We postulate that ZRF1 operates in conjunction with cellular remodeling machines and suggest that on-site remodeling might be a hallmark of many chromatin-associated signaling pathways. We discuss yet unexplored functions of ZRF1-mediated remodeling in replication and double strand break repair. In conclusion, we postulate that on-site remodeling of multiprotein complexes is essential for the timing of chromatin signaling processes.

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Nucleotide excision repair leaves a mark on chromatin: DNA damage detection in nucleosomes

Apelt

Lans

Schärer

et al. 2021

Cell. Mol. Life Sci.

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Global genome nucleotide excision repair (GG-NER) eliminates a broad spectrum of DNA lesions from genomic DNA. Genomic DNA is tightly wrapped around histones creating a barrier for DNA repair proteins to access DNA lesions buried in nucleosomal DNA. The DNA-damage sensors XPC and DDB2 recognize DNA lesions in nucleosomal DNA and initiate repair. The emerging view is that a tight interplay between XPC and DDB2 is regulated by post-translational modifications on the damage sensors themselves as well as on chromatin containing DNA lesions. The choreography between XPC and DDB2, their interconnection with post-translational modifications such as ubiquitylation, SUMOylation, methylation, poly(ADP-ribos)ylation, acetylation, and the functional links with chromatin remodelling activities regulate not only the initial recognition of DNA lesions in nucleosomes, but also the downstream recruitment and necessary displacement of GG-NER factors as repair progresses. In this review, we highlight how nucleotide excision repair leaves a mark on chromatin to enable DNA damage detection in nucleosomes.

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ZRF1 mediates remodeling of E3 ligases at DNA lesion sites during nucleotide excision repair

Cited by 38 publications

References 55 publications

Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

On‐site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation

Nucleotide excision repair leaves a mark on chromatin: DNA damage detection in nucleosomes

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