The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
Open accessAbstract
Through a genetic screen using myosin-like protein strains mlp1 Δ mlp2 Δ and biochemical purification, we identified a complex of eight proteins, each required for growth and DNA repair in Saccharomyces cerevisiae . Among the subunits are Mms21 that contains a putative Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING domain characteristic of small ubiquitin-like m o difier (SUMO) ligases, two structural-maintenance-of-chromosome (Smc) proteins, Smc5 and Smc6, and a protein that contains an ubiquitin ligase signature domain. We show that these proteins colocalized to several distinct nuclear foci. Biochemical and genetic data demonstrated that Mms21 indeed functions as a SUMO ligase and that this activity requires the Siz/PIAS (protein inhibitor of activated signal transducer and activator of transcription) RING domain. The substrates for this SUMO ligase include a subunit of the octameric complex, Smc5, and the DNA repair protein Yku70. We further show that the abolition of the SUMO E3 activity of Mms21 leads to such disparate phenotypes as DNA damage sensitivity, defects in nucleolar integrity and telomere clustering, silencing, and length regulation. We propose that Mms21 sumoylates proteins involved in these diverse processes and that the other members of the complex, particularly Smc5/6, facilitate proper substrate sumoylation by localizing Mms21 to specific chromosomal regions.
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Cites
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
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Sumo, ubiquitin's mysterious cousin
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Cited by
Regulation of DNA repair throughout the cell cycle
Branzei, D., & Foiani, M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2351 · Cited by 1,228
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092
Maintaining genome stability at the replication fork
Branzei, D., & Foiani, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2852 · Cited by 786
The nuclear envelope and transcriptional control
Akhtar, A., & Gasser, S. M. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2122 · Cited by 441
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
Morris, J. R., Boutell, C., Keppler, M., Densham, R., Weekes, D., Alamshah, A., Butler, L., Galanty, Y., Pangon, L., Kiuchi, T., et al. (2009) · Nature · doi:10.1038/nature08593 · Cited by 375
Metadata
- Authors
- Zhao, X., & Blobel, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-02-28
- Volume
- 102
- Issue
- 13
- Pages
- 4777-4782
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1600888450
- Cited by
- 458
- References
- 40
- FWCI
- 10.83
- Type
- journal article
- Language
- en
- Open access
- green
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- Zhao, X., & Blobel, G. (2005). A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0500537102
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