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The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons
by
Herbert, Alan
in
Acids
/ Argonaute Proteins - chemistry
/ Argonaute Proteins - metabolism
/ Chromatin
/ Chromosomal proteins
/ DNA
/ DNA - chemistry
/ DNA - metabolism
/ Genomes
/ HMGB1 Protein - chemistry
/ HMGB1 Protein - metabolism
/ Humans
/ Interferon
/ MicroRNA
/ Models, Molecular
/ Nematodes
/ Nucleic Acid Conformation
/ Pathogens
/ Protein Binding
/ Proteins
/ RNA polymerase
/ RNA, Untranslated - chemistry
/ RNA, Untranslated - genetics
/ RNA, Untranslated - metabolism
/ Transcription factors
/ Tumor proteins
/ Tumor Suppressor Protein p53 - chemistry
/ Tumor Suppressor Protein p53 - metabolism
/ Vertebrates
2026
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The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons
by
Herbert, Alan
in
Acids
/ Argonaute Proteins - chemistry
/ Argonaute Proteins - metabolism
/ Chromatin
/ Chromosomal proteins
/ DNA
/ DNA - chemistry
/ DNA - metabolism
/ Genomes
/ HMGB1 Protein - chemistry
/ HMGB1 Protein - metabolism
/ Humans
/ Interferon
/ MicroRNA
/ Models, Molecular
/ Nematodes
/ Nucleic Acid Conformation
/ Pathogens
/ Protein Binding
/ Proteins
/ RNA polymerase
/ RNA, Untranslated - chemistry
/ RNA, Untranslated - genetics
/ RNA, Untranslated - metabolism
/ Transcription factors
/ Tumor proteins
/ Tumor Suppressor Protein p53 - chemistry
/ Tumor Suppressor Protein p53 - metabolism
/ Vertebrates
2026
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The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons
by
Herbert, Alan
in
Acids
/ Argonaute Proteins - chemistry
/ Argonaute Proteins - metabolism
/ Chromatin
/ Chromosomal proteins
/ DNA
/ DNA - chemistry
/ DNA - metabolism
/ Genomes
/ HMGB1 Protein - chemistry
/ HMGB1 Protein - metabolism
/ Humans
/ Interferon
/ MicroRNA
/ Models, Molecular
/ Nematodes
/ Nucleic Acid Conformation
/ Pathogens
/ Protein Binding
/ Proteins
/ RNA polymerase
/ RNA, Untranslated - chemistry
/ RNA, Untranslated - genetics
/ RNA, Untranslated - metabolism
/ Transcription factors
/ Tumor proteins
/ Tumor Suppressor Protein p53 - chemistry
/ Tumor Suppressor Protein p53 - metabolism
/ Vertebrates
2026
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The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons
Journal Article
The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons
2026
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Overview
Triplexes (TRX) are a class of flipons that can form due to the interaction of RNA with B-DNA. While many proteins have been proposed to bind triplexes, structural models of these interactions do not exist. Here, I present AlphaFold V3 (AF3) models that reveal interactions between the high-mobility group protein B1 (HMGB1), HNRNPU (SAF-A), TP53, ARGONAUTE (AGO), and REL domain proteins. The TRXs result from the sequence-specific docking of RNAs to DNA via Hoogsteen base pairing. The RNA and DNA strands in apolar TRX are oriented in the opposite 5′ to 3′ direction, while copolar TRX have RNA and DNA strands pointing in the same 5′ to 3′ direction. TRXs can incorporate different RNA classes, including long noncoding RNAs (lncRNAs), short RNAs, such as miRNAs, piRNAs, and tRNAs, nascent RNA fragments, and non-canonical base triplets. Many pathways regulated by TRX formation have evolved to constrain retroelements (EREs), which are both an existential threat to the host and a source of genotypic variation. TRXs help set the boundaries of active chromatin, repressing the expression of most EREs, while depending on other flipons to modulate cellular programs. The TRXs help nucleate folding of intrinsically disordered proteins.
Publisher
MDPI AG,Multidisciplinary Digital Publishing Institute (MDPI)
Subject
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