ArticleProceedings of the National Academy of Sciences of the United States of America2009
Tetramer opening in LacI-mediated DNA looping.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 51 citations in OpenAlex.
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- T3SS protein EsrC binds to theApplied and environmental microbiology · 2024Article
- The intracellular visualization of exogenous DNA in fluorescence microscopy.Drug delivery and translational research · 2024Review
- Detecting DNA Loops Using Tethered Particle Motion.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Atlas: automatic modeling of regulation of bacterial gene expression and metabolism using rule-based languages.Bioinformatics (Oxford, England) · 2021Article
- When is a transcription factor a NAP?Current opinion in microbiology · 2020Review
- Tethered multifluorophore motion reveals equilibrium transition kinetics of single DNA double helices.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Sliding of a single lac repressor protein along DNA is tuned by DNA sequence and molecular switching.Nucleic acids research · 2018Article
- Structure-guided approach to site-specific fluorophore labeling of the lac repressor LacI.PloS one · 2018Article
- The MalR type regulator AcrC is a transcriptional repressor of acarbose biosynthetic genes in Actinoplanes sp. SE50/110.BMC genomics · 2017Article
- Proteins mediating DNA loops effectively block transcription.Protein science : a publication of the Protein Society · 2017Article
- Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox Proteins.The Journal of biological chemistry · 2015Review
- Combining single-molecule manipulation and imaging for the study of protein-DNA interactions.Journal of visualized experiments : JoVE · 2014Article
- Tethered particle motion reveals that LacI·DNA loops coexist with a competitor-resistant but apparently unlooped conformation.Biophysical journal · 2014Article
- Enhanced tethered-particle motion analysis reveals viscous effects.Biophysical journal · 2014Article
- Multiple LacI-mediated loops revealed by Bayesian statistics and tethered particle motion.Nucleic acids research · 2014Article
- Rationally designed coiled-coil DNA looping peptides control DNA topology.Nucleic acids research · 2013Article
- DNA looping in prokaryotes: experimental and theoretical approaches.Journal of bacteriology · 2013Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
Abstract
Lactose repressor protein (LacI) controls transcription of the genes involved in lactose metabolism in bacteria. Essential to optimal LacI-mediated regulation is its ability to bind simultaneously to two operators, forming a loop on the intervening DNA. Recently, several lines of evidence (both theoretical and experimental) have suggested various possible loop structures associated with different DNA binding topologies and LacI tetramer structural conformations (adopted by flexing about the C-terminal tetramerization domain). We address, specifically, the role of protein opening in loop formation by employing the single-molecule tethered particle motion method on LacI protein mutants chemically cross-linked at different positions along the cleft between the two dimers. Measurements on the wild-type and uncross-linked LacI mutants led to the observation of two distinct levels of short tether length, associated with two different DNA looping structures. Restricting conformational flexibility of the protein by chemical cross-linking induces pronounced effects. Crosslinking the dimers at the level of the N-terminal DNA binding head (E36C) completely suppresses looping, whereas cross-linking near the C-terminal tetramerization domain (Q231C) results in changes of looping geometry detected by the measured tether length distributions. These observations lead to the conclusion that tetramer opening plays a definite role in at least a subset of LacI/DNA loop conformations.
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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.