ArticleBMC research notes2010
SUMO-1 possesses DNA binding activity.
Article in BMC research notes, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The trial behind it
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- FAM111A regulates replication origin activation and cell fitness.Life science alliance · 2023Article
- Sumoylation of Cas9 at lysine 848 regulates protein stability and DNA binding.Life science alliance · 2022Article
- Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1.Structure (London, England : 1993) · 2020Article
- Olig2 SUMOylation protects against genotoxic damage response by antagonizing p53 gene targeting.Cell death and differentiation · 2020Article
- Identification of a noncanonical RNA binding domain in the U2 snRNP protein SF3A1.RNA (New York, N.Y.) · 2019Article
- SUMOylation of HP1α supports association with ncRNA to define responsiveness of breast cancer cells to chemotherapy.Oncotarget · 2016Article
- SUMO-mediated regulation of DNA damage repair and responses.Trends in biochemical sciences · 2015Review
- Hes-1 SUMOylation by protein inhibitor of activated STAT1 enhances the suppressing effect of Hes-1 on GADD45α expression to increase cell survival.Journal of biomedical science · 2014Article
- Two-way communications between ubiquitin-like modifiers and DNA.Nature structural & molecular biology · 2014Review
- A TDG/CBP/RARα ternary complex mediates the retinoic acid-dependent expression of DNA methylation-sensitive genes.Genomics, proteomics & bioinformatics · 2014Article
- SUMO1 modification of PTEN regulates tumorigenesis by controlling its association with the plasma membrane.Nature communications · 2012Article
- SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.BMC biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundConjugation of small ubiquitin-related modifiers (SUMOs) is a frequent post-translational modification of proteins. SUMOs can also temporally associate with protein-targets via SUMO binding motifs (SBMs). Protein sumoylation has been identified as an important regulatory mechanism especially in the regulation of transcription and the maintenance of genome stability. The precise molecular mechanisms by which SUMO conjugation and association act are, however, not understood.
findingsUsing NMR spectroscopy and protein-DNA cross-linking experiments, we demonstrate here that SUMO-1 can specifically interact with dsDNA in a sequence-independent fashion. We also show that SUMO-1 binding to DNA can compete with other protein-DNA interactions at the example of the regulatory domain of Thymine-DNA Glycosylase and, based on these competition studies, estimate the DNA binding constant of SUMO1 in the range 1 mM.
conclusionThis finding provides an important insight into how SUMO-1 might exert its activity. SUMO-1 might play a general role in destabilizing DNA bound protein complexes thereby operating in a bottle-opener way of fashion, explaining its pivotal role in regulating the activity of many central transcription and DNA repair complexes.
Identifiers
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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.