ArticleScientific reports2019
Structures of GapR reveal a central channel which could accommodate B-DNA.
Article in Scientific reports, 2019. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed.
- GapR stiffens AT-rich and overtwisted DNA leading to differential effects on transcription based on gene context.Nucleic acids research · 2026Article
- Metagenomic approaches for studying ubiquitous yet diverse nucleoid associated proteins in microbial communities: challenges and advances.World journal of microbiology & biotechnology · 2025Review
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Two novel phages infectingFrontiers in microbiology · 2025Article
- Article
- Bacterial chromatin proteins, transcription, and DNA topology: Inseparable partners in the control of gene expression.Molecular microbiology · 2024Review
- The DNA Recognition Motif of GapR Has an Intrinsic DNA Binding Preference towards AT-rich DNA.Molecules (Basel, Switzerland) · 2021Article
- Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom.Transcription · 2021Review
- Article
- Jumbo Phages: A Comparative Genomic Overview of Core Functions and Adaptions for Biological Conflicts.Viruses · 2021Article
- GapR binds DNA through dynamic opening of its tetrameric interface.Nucleic acids research · 2020Article
- Chromatin Architectural Factors as Safeguards against Excessive Supercoiling during DNA Replication.International journal of molecular sciences · 2020Review
- The Nucleoid-Associated Protein GapR Uses Conserved Structural Elements To Oligomerize and Bind DNA.mBio · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
GapR is a nucleoid-associated protein required for the cell cycle of Caulobacter cresentus. We have determined new crystal structures of GapR to high resolution. As in a recently published structure, a GapR monomer folds into one long N-terminal α helix and two shorter α helices, and assembles into a tetrameric ring with a closed, positively charged, central channel. In contrast to the conclusions drawn from the published structures, we observe that the central channel of the tetramer presented here could freely accommodate B-DNA. Mutation of six conserved lysine residues lining the cavity and electrophoretic mobility gel shift experiments confirmed their role in DNA binding and the channel as the site of DNA binding. Although present in our crystals, DNA could not be observed in the electron density maps, suggesting that DNA binding is non-specific, which could be important for tetramer-ring translocation along the chromosome. In conjunction with previous GapR structures we propose a model for DNA binding and translocation that explains key published observations on GapR and its biological functions.
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Registered trials
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