ArticleMolecular and cellular biology1997
Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 107 citations in OpenAlex.
- Overlapping RAD18-and DNA-binding interfaces in DNA polymerase η contribute to UV-induced DNA damage tolerance.The Journal of biological chemistry · 2026Article
- Molecular basis for PHF7-mediated ubiquitination of histone H3.Genes & development · 2023Article
- A series of xanthenes inhibiting Rad6 function and Rad6-Rad18 interaction in the PCNA ubiquitination cascade.iScience · 2022Article
- The Zn-finger of Saccharomyces cerevisiae Rad18 and its adjacent region mediate interaction with Rad5.G3 (Bethesda, Md.) · 2021Article
- Article
- Balancing self-renewal against genome preservation in stem cells: How do they manage to have the cake and eat it too?Cellular and molecular life sciences : CMLS · 2016Review
- Monoubiquitination of histone H2B is intrinsic to the Bre1 RING domain-Rad6 interaction and augmented by a second Rad6-binding site on Bre1.The Journal of biological chemistry · 2015Article
- Regulation of Rad6/Rad18 Activity During DNA Damage Tolerance.Annual review of biophysics · 2015Review
- Role of E2-Ub-conjugating enzymes during skeletal muscle atrophy.Frontiers in physiology · 2015Review
- SIVA1 directs the E3 ubiquitin ligase RAD18 for PCNA monoubiquitination.The Journal of cell biology · 2014Article
- RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination.Biochimica et biophysica acta · 2014Review
- In vivo and in silico analysis of PCNA ubiquitylation in the activation of the Post Replication Repair pathway in S. cerevisiae.BMC systems biology · 2013Article
- Asymmetric nature of two subunits of RAD18, a RING-type ubiquitin ligase E3, in the human RAD6A-RAD18 ternary complex.Nucleic acids research · 2012Article
- RAD6 regulates the dosage of p53 by a combination of transcriptional and posttranscriptional mechanisms.Molecular and cellular biology · 2012Article
- E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- E2 ligase dRad6 regulates DMP53 turnover in Drosophila.The Journal of biological chemistry · 2011Article
- Human RAD18 interacts with ubiquitylated chromatin components and facilitates RAD9 recruitment to DNA double strand breaks.PloS one · 2011Article
- E2s: structurally economical and functionally replete.The Biochemical journal · 2011Review
- Utility of DNA postreplication repair protein Rad6B in neoadjuvant chemotherapy response.Medical oncology (Northwood, London, England) · 2010Article
- Building ubiquitin chains: E2 enzymes at work.Nature reviews. Molecular cell biology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin-conjugating enzyme required for postreplicational repair of UV-damaged DNA and for damage-induced mutagenesis. In addition, Rad6 functions in the N end rule pathway of protein degradation. Rad6 mediates its DNA repair role via its association with Rad18, whose DNA binding activity may target the Rad6-Rad18 complex to damaged sites in DNA. In its role in N end-dependent protein degradation, Rad6 interacts with the UBR1-encoded ubiquitin protein ligase (E3) enzyme. Previous studies have indicated the involvement of N-terminal and C-terminal regions of Rad6 in interactions with Ubr1. Here, we identify the regions of Rad6 and Rad18 that are involved in the dimerization of these two proteins. We show that a region of 40 amino acids towards the C terminus of Rad18 (residues 371 to 410) is sufficient for interaction with Rad6. This region of Rad18 contains a number of nonpolar residues that have been conserved in helix-loop-helix motifs of other proteins. Our studies indicate the requirement for residues 141 to 149 at the C terminus, and suggest the involvement of residues 10 to 22 at the N terminus of Rad6, in the interaction with Rad18. Each of these regions of Rad6 is indicated to form an amphipathic helix.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.