2024
Identifying topologically associating domains using differential kernels
Maisuradze L, King M, Surovtsev I, Mochrie S, Shattuck M, O’Hern C. Identifying topologically associating domains using differential kernels. PLOS Computational Biology 2024, 20: e1012221. PMID: 39008525, PMCID: PMC11249266, DOI: 10.1371/journal.pcbi.1012221.Peer-Reviewed Original ResearchConceptsTopologically associating domainsHi-C mapsFalse discovery rateChromatin conformation capture techniquesEnhancer-promoter interactionsLow false discovery rateSelf-interacting regionsStructure of chromatinRegulate gene expressionAverage contact probabilitiesHi-CLocus IDNA transcriptionGene expressionChromatinDiscovery rateContact probabilityBiological phenomenaState-of-the-artKernel-based techniqueComputer visionReplicationCorrelated changesDisease statesCapture techniquesEffect of loops on the mean-square displacement of Rouse-model chromatin
Yuan T, Yan H, Bailey M, Williams J, Surovtsev I, King M, Mochrie S. Effect of loops on the mean-square displacement of Rouse-model chromatin. Physical Review E 2024, 109: 044502. PMID: 38755928, DOI: 10.1103/physreve.109.044502.Peer-Reviewed Original ResearchConceptsStretching exponentConsistent with recent experimentsTopologically associating domainsMean square displacementRecent experimentsLoop extrusionExponent valuesTAD formationTree of lifeDynamics of chromatinExponentEffects of loopChromatin lociChromatin dynamicsRouse modelChromatin organizationChromatin mobilityGene locusContact mapsDynamicsChromatinLoopPolymer dynamicsLociPolymer simulations
2023
Acetyl-methyllysine marks chromatin at active transcription start sites
Lu-Culligan W, Connor L, Xie Y, Ekundayo B, Rose B, Machyna M, Pintado-Urbanc A, Zimmer J, Vock I, Bhanu N, King M, Garcia B, Bleichert F, Simon M. Acetyl-methyllysine marks chromatin at active transcription start sites. Nature 2023, 622: 173-179. PMID: 37731000, PMCID: PMC10845139, DOI: 10.1038/s41586-023-06565-9.Peer-Reviewed Original ResearchConceptsPost-translational modificationsLysine residuesActive transcription start sitesTranscription start siteRange of speciesChromatin biologyChromatin proteinsLysine methylationActive chromatinProteins BRD2Transcriptional initiationLysine acetylationHistone H4Start siteMammalian tissuesHuman diseasesSame residuesMethylationAcetylationChromatinResiduesProteinBiological signalsHistonesBRD2Loops and the activity of loop extrusion factors constrain chromatin dynamics
Bailey M, Surovtsev I, Williams J, Yan H, Yuan T, Li K, Duseau K, Mochrie S, King M. Loops and the activity of loop extrusion factors constrain chromatin dynamics. Molecular Biology Of The Cell 2023, 34: ar78. PMID: 37126401, PMCID: PMC10398873, DOI: 10.1091/mbc.e23-04-0119.Peer-Reviewed Original ResearchConceptsChromatin dynamicsChromatin mobilityChromatin conformation capture experimentsINO80 chromatin remodelerSystematic genetic perturbationsDynamics of chromatinSWI/SNFChromatin fluctuationsCondensin complexRSC complexChromatin remodelersFission yeastChromosome structureChromatin polymerExtrusion factorsChromatin motionGenetic perturbationsThree-dimensional structureDNA structureChromatinCohesinPolymer simulationsIntroduction of loopsKey roleActive process
2018
Integration of Biochemical and Mechanical Signals at the Nuclear Periphery: Impacts on Skin Development and Disease
Stewart R, King M, Horsley V. Integration of Biochemical and Mechanical Signals at the Nuclear Periphery: Impacts on Skin Development and Disease. Stem Cell Biology And Regenerative Medicine 2018, 263-292. DOI: 10.1007/978-3-319-16769-5_11.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsNuclear laminaIntegral inner nuclear membrane proteinsInner nuclear membrane proteinSkin developmentMechanical signalsNuclear membrane proteinsInner nuclear membraneIntegration of biochemicalGenome integrityNuclear peripheryTranscriptional outputNuclear laminsAssociated chromatinMembrane proteinsNuclear interiorTissue-level mechanicsGene expressionNuclear membraneSkin homeostasisKeratinocyte differentiationMechanical inputChromatinLaminsLaminaProtein
2015
The tethering of chromatin to the nuclear envelope supports nuclear mechanics
Schreiner SM, Koo PK, Zhao Y, Mochrie SG, King MC. The tethering of chromatin to the nuclear envelope supports nuclear mechanics. Nature Communications 2015, 6: 7159. PMID: 26074052, PMCID: PMC4490570, DOI: 10.1038/ncomms8159.Peer-Reviewed Original ResearchConceptsNuclear mechanicsRole of chromatinOptical tweezersWild-type nucleiNetwork of lipidsCytoskeletal forcesNuclear laminaCytoskeletal dynamicsMechanical defensesMembrane tethersDeformable nucleiNuclear envelopeChromatinNuclear shapeIsolated nucleiIndividual mechanical contributionsMembrane resultsNucleusTweezersMechanicsLaminsProteinTetheringLaminaDefense