ArticleBiochemical and biophysical research communications2008
Interactions of recombinant HMGB proteins with branched RNA substrates.
Article in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- HMGB1 prefers to interact with structural RNAs and regulates rRNA methylation modification and translation in HeLa cells.BMC genomics · 2024Article
- Negatively charged, intrinsically disordered regions can accelerate target search by DNA-binding proteins.Nucleic acids research · 2023Article
- Interactions of HMGB Proteins with the Genome and the Impact on Disease.Biomolecules · 2021Review
- RAGE Enhances TLR Responses through Binding and Internalization of RNA.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- The cis-acting replication element of the Hepatitis C virus genome recruits host factors that influence viral replication and translation.Scientific reports · 2016Article
- Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Biochimica et biophysica acta · 2015Review
- Mitochondrial Transcription Factor A (TFAM) Binds to RNA Containing 4-Way Junctions and Mitochondrial tRNA.PloS one · 2015Article
- A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.PloS one · 2015Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Interaction of HMG proteins and H1 with hybrid PNA-DNA junctions.Protein science : a publication of the Protein Society · 2013Article
- Article
- A phage RNA-binding protein binds to a non-cognate structured RNA and stabilizes its core structure.Biochemical and biophysical research communications · 2009Article
- The DNA binding high mobility group box protein family functionally binds RNA.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The high mobility group protein HMGB1 is a highly abundant chromosomal protein known to interact preferentially with DNA that is branched, bent or otherwise structurally altered. Biologically the protein is thought to facilitate promoter attachment by transcription factors. Recently, however, HMGB1 has been shown to have biological roles beyond that of an architectural DNA-binding protein. Here we investigate the binding interactions of recombinant HMGB1 proteins with two branched RNA's E. coli 5S rRNA and the group I intron ribozyme from Azoarcus pre-tRNA(Ile). Using competitive electrophoretic mobility and circular dichroism binding assays, we show that HMGB proteins bind both substrates with high affinity. We also report that a recombinant rat HMGB protein, rHMGB1b, inhibits RNA cleavage by the ribozyme. These results raise the possibility that HMGB proteins possess structure dependent RNA binding activity and can modulate RNA processing as well as transcription.
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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.