ArticleNucleic acids research2009
Regulation of UMSBP activities through redox-sensitive protein domains.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- CRISPR/Cas9-mediated deletion of a kinetoplast-associated gene attenuates virulence in Leishmania major parasites.Medical microbiology and immunology · 2025Article
- Mitochondrial genome maintenance-the kinetoplast story.FEMS microbiology reviews · 2023Review
- UMSBP2 is chromatin remodeler that functions in regulation of gene expression and suppression of antigenic variation in trypanosomes.Nucleic acids research · 2023Article
- Genome-scale RNA interference profiling of Trypanosoma brucei cell cycle progression defects.Nature communications · 2022Article
- Direct monitoring of the stepwise condensation of kinetoplast DNA networks.Scientific reports · 2021Article
- Molecular and Functional Characteristics of DNA Polymerase Beta-Like Enzymes From Trypanosomatids.Frontiers in cellular and infection microbiology · 2021Review
- Trypanosoma brucei UMSBP2 is a single-stranded telomeric DNA binding protein essential for chromosome end protection.Nucleic acids research · 2018Article
- Universal minicircle sequence binding protein of Leishmania donovani regulates pathogenicity by controlling expression of cytochrome-b.Cell & bioscience · 2016Article
- Interactions of a replication initiator with histone H1-like proteins remodel the condensed mitochondrial genome.The Journal of biological chemistry · 2011Article
- Genomic organization of leishmania species.Iranian journal of parasitology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UMSBP is a CCHC-type zinc finger protein, which functions during replication initiation of kinetoplast DNA minicircles and the segregation of kinetoplast DNA networks. Interactions of UMSBP with origin sequences, as well as the protein oligomerization, are affected by its redox state. Reduction yields UMSBP monomers and activates its binding to DNA, while oxidation drives UMSBP oligomerization and impairs its DNA-binding activity. Kinetics analyses of UMSBP-DNA interactions revealed that redox affects the association of free UMSBP with the DNA, but has little effect on its dissociation from the nucleoprotein complex. A previously proposed model, suggesting that binding of DNA is regulated via the reversible interconversions of active UMSBP monomers and inactive oligomers, was challenged here, revealing that the two redox-driven processes are not interrelated. No correlation could be observed between DNA-binding inhibition and UMSBP oligomerization, upon oxidation of UMSBP. Moreover, while the presence of zinc ions was found to be essential for the interaction of UMSBP with DNA, UMSBP oligomerization occurred through zinc-depleted, unfolded zinc finger domains. Site directed mutagenesis analysis of UMSBP suggested that its unique methionine residue, which can be oxidized into methionine sulfoxide, is not involved in the redox-mediated regulation of UMSBP-DNA interactions.
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