Shoichi Tachiyama
Postdoctoral AssociateDownloadHi-Res Photo
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Postdoctoral Associate
Biography
Dr. Tachiyama earned his Ph.D. in Biochemistry and Biophysics at the University of Kansas in 2020. In his Ph.D. projects, he used biophysical and microbiological approaches to research molecular functions and protein interactions on the cytoplasmic side of the Shigella type III secretion system. In 2020, he joined Dr. Jun Liu’s laboratory at Yale and has continued to research the Shigella T3SS in situ. This research project is conducted in collaboration with Dr. William Picking, University of Kansas. Dr. Tachiyama’s work also focuses on structural details of the flagellar motor in Helicobacter pylori using in-situ approaches, in collaboration with Dr. Timothy Hoover, University of Georgia.
Appointments
Microbial Pathogenesis
Postdoctoral AssociatePrimary
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Research
Overview
Medical Research Interests
Cryoelectron Microscopy; Flagella; Host-Pathogen Interactions; Molecular Structure
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Liu Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of Shoichi Tachiyama's published research.
Publications Timeline
A big-picture view of Shoichi Tachiyama's research output by year.
Research Interests
Research topics Shoichi Tachiyama is interested in exploring.
Jun Liu, PhD
Aimilia Krypotou
Andrew Goodman, PhD
Eduardo Groisman, PhD
Nick Pokorzynski, PhD
7Publications
123Citations
Publications
2024
Bacterial flagella hijack type IV pili proteins to control motility
Liu X, Tachiyama S, Zhou X, Mathias R, Bonny S, Khan M, Xin Y, Roujeinikova A, Liu J, Ottemann K. Bacterial flagella hijack type IV pili proteins to control motility. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2317452121. PMID: 38236729, PMCID: PMC10823254, DOI: 10.1073/pnas.2317452121.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and Concepts
2023
FlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori
Botting J, Tachiyama S, Gibson K, Liu J, Starai V, Hoover T. FlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori. PLOS ONE 2023, 18: e0287514. PMID: 37976320, PMCID: PMC10655999, DOI: 10.1371/journal.pone.0287514.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsBacteria require phase separation for fitness in the mammalian gut
Krypotou E, Townsend G, Gao X, Tachiyama S, Liu J, Pokorzynski N, Goodman A, Groisman E. Bacteria require phase separation for fitness in the mammalian gut. Science 2023, 379: 1149-1156. PMID: 36927025, PMCID: PMC10148683, DOI: 10.1126/science.abn7229.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMammalian gutTranscription termination factor RhoTermination factor RhoGene regulationTranscription terminationMechanisms bacteriaBacteria interactionsHuman commensalValuable targetBacteriaRhoGut microbiotaFitnessNovel clinical applicationsTherapeutic manipulationGutHuman healthCommensalRegulation
2021
Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System
Tachiyama S, Skaar R, Chang Y, Carroll BL, Muthuramalingam M, Whittier SK, Barta ML, Picking WL, Liu J, Picking WD. Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System. Frontiers In Cellular And Infection Microbiology 2021, 11: 682635. PMID: 34150677, PMCID: PMC8211105, DOI: 10.3389/fcimb.2021.682635.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsType III secretion systemCytoplasmic sorting platformSorting platformSecretion systemTwo-hybrid analysisCryo-electron tomography dataC-terminal domainShigella type III secretion systemFull-length copiesBiophysical propertiesDistinct biophysical propertiesSpa47 ATPaseT3SS injectisomeEffector proteinsSecretion substratesDistinct complexesIntracellular nicheBasal bodiesPrimary virulence factorSpa33Host cellsHeterotrimerPrecise makeupVirulence factorsMxiK
2020
The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform
Muthuramalingam M, Whittier SK, Lovell S, Battaile KP, Tachiyama S, Johnson DK, Picking WL, Picking WD. The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform. Journal Of Molecular Biology 2020, 432: 166693. PMID: 33122003, PMCID: PMC10550303, DOI: 10.1016/j.jmb.2020.10.027.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsInner membrane ringBasal bodiesCytoplasmic domainSorting platformFirst high-resolution structureType III secretion systemCytoplasmic sorting platformTwo-hybrid analysisGram-negative bacterial pathogensProtein family membersNormal cellular functionHigh-resolution structuresAtomic resolution modelsHelix-rich structureEukaryotic cellsT3SS apparatusAdaptor proteinCellular functionsSecretion systemMembrane ringMechanistic interfaceTip complexExternal needleRadial spokesProtein
2019
The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system
Tachiyama S, Chang Y, Muthuramalingam M, Hu B, Barta ML, Picking WL, Liu J, Picking WD. The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system. Journal Of Biological Chemistry 2019, 294: 19184-19196. PMID: 31699894, PMCID: PMC6916477, DOI: 10.1074/jbc.ra119.009125.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsInner membrane ringType III secretion systemCytoplasmic domainSecretion systemCytoplasmic sorting platformForkhead-associated (FHA) domainShigella type III secretion systemDiverse bacterial pathogensDisruption of interactionsSpa47 ATPaseStructure-function relationshipsExtracellular needleEffector recognitionGram-negative bacteriaEukaryotic cellsT3SS apparatusVirulence effectorsMembrane ringSorting platformInsertional mutagenesisGenetic methodsHomologous interactionsMxiKTip complexBasal bodies
2018
Using disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB
Barta ML, Tachiyama S, Muthuramalingam M, Arizmendi O, Villanueva CE, Ramyar KX, Geisbrecht BV, Lovell S, Battaile KP, Picking WL, Picking WD. Using disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB. Protein Science 2018, 27: 1392-1406. PMID: 29672980, PMCID: PMC6153406, DOI: 10.1002/pro.3428.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsTip complexInsertional mutagenesisTranslocator protein IpaBBacterial type III secretion systemType III secretion systemC-terminal halfN-terminal halfInsertion mutantsT3SS apparatusCellular functionsLatter mutantSecretion inductionMammalian cellsSecretion systemTC functionHost membraneBasal bodiesBacteriophage T4 lysozymeTertiary structureImpaired interactionIpaBPore formationT4 lysozymeBacterial surfaceMutants