Budding yeast Rad9 is an ATP-dependent Rad53 activating machine
Open accessAbstract
We find budding yeast Rad9 in two distinct, large, and soluble complexes in cell extracts. The larger (> or =850 kDa) complex, found in nondamaged cells, contains hypophosphorylated Rad9, whereas the smaller (560 kDa) complex, which forms after DNA damage, contains hyperphosphorylated Rad9 and Rad53. This smaller Rad9 complex is capable of catalyzing phosphorylation and release of active Rad53 kinase, a process requiring the kinase activity of Rad53. However, Mec1 and Tel1 are no longer required once the 560 kDa complex has been formed. We propose a model whereby Mec1/Tel1-dependent hyperphosphorylation of Rad9 results in formation of the smaller Rad9 complex and recruitment of Rad53. This complex then catalyzes activation of Rad53 by acting as a scaffold that brings Rad53 molecules into close proximity, facilitating Rad53 in trans autophosphorylation and subsequent release of activated Rad53.
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Rad9 oligomerization is critical for scaffolding Rad53 binding, increasing local Rad53 concentration and stimulating autophosphorylation, leading to full Rad53 activation.
“Oligomerization of Rad9 seems to be critical to provide a scaffold for Rad53 binding, leading to a local increase in Rad53 molecules and stimulating its auto-phosphorylation; this event is responsible for full Rad53 activation [28,29].”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [29]
Rad9 phosphorylation by the apical kinase recruits Rad53 to the damage site, allowing Mec1 to phosphorylate it.
“The prototype of checkpoint mediators is S. cerevisiae Rad9, which, once phosphorylated by the apical kinase, recruits Rad53 at the damage site allowing its phosphorylation by Mec1.”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [29]
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References 36 · Cited by 296
- Authors
- Gilbert, C. S., Green, C. M., & Lowndes, N. F.
- Affiliations
- Ollscoil na Gaillimhe – University of Galway (IE)
- Corresponding author
- Lowndes, Noel F
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2001-07
- Volume
- 8
- Issue
- 1
- Pages
- 129-136
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2069334332
- Cited by
- 296
- References
- 36
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 4 · 2023: 7 · 2022: 5 · 2021: 6 · 2020: 6 · 2019: 7 · 2018: 5 · 2017: 4 · 2016: 11 · 2015: 7 · 2014: 7 · 2013: 15 · 2012: 6
- FWCI
- 10.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) (acceptedVersion, cc-by-nc-nd)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion)
- ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) (submittedVersion, cc-by-nc-nd)
- ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) (submittedVersion, cc-by-nc)
- Research Repository UCD (University College Dublin) (cc-by-nc)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- Rad9, Rad53, DNA damage response, Mec1, Tel1, Saccharomyces cerevisiae
- MeSH terms
- Adenosine Triphosphate, Cell Cycle, DNA Repair, Saccharomycetales, Fungal Proteins, Models, Biological, Phosphorylation, Recombinant Proteins, Immunoblotting, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, Macromolecular Substances, Intracellular Signaling Peptides and Proteins, Checkpoint Kinase 2
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