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Jonathan Lynch, Ph.D.

Description of Research

Animals are intimately associated with communities of microorganisms collectively referred to as the microbiota. The bacteria, archaea, fungi, and viruses that make up the animal microbiota profoundly shape the physiology of their host, altering host metabolism, immune function, and development. This powerfully positions the microbiota as a tool that we can use to influence host biology in meaningful ways.

However, the microbiota is incredibly complex, making it difficult to properly describe, let alone to intentionally manipulate. This is especially true with the gastrointestinal/gut microbiota, where hundreds of poorly characterized microbial species that vary across hosts collectively shape host physiology at multiple levels. Still, the foundations of these complex relationships are shared across different hosts and different contexts, so it is often possible to generalize specific mechanisms across unique microbiotas.

The lab of Host-Microbe Dynamics works to define the fundamental principles of symbiotic relationships between animals and their microbiota. We focus on how the microbiota senses, responds to, and interacts with host lipid metabolism, neurotransmitters, and physical parameters. Ultimately, our goal is to better define the host-microbe relationship and to understand how we can exploit the microbiota to improve host health.

Lab Members

  • Grace Heiting, research technologist, Department of Biological Chemistry
  • Tanae Lewis, graduate student, GPBC
  • Kamal Kaur, undergraduate student
  • Sarah Rosental, undergraduate student

Publications

§=corresponding, *=these authors contributed equally

  • Jonathan B. Lynch§, Gonzalez EL, Choy K, Faull KF, Jewell T, Arrellano A, Liang J, Yu KB, Paramo J, Hsiao EY. Gut microbiota Turicibacter strains differentially modify bile acids and host lipids. Nature Communications 14(3669), 2023. bioRxiv https://www.biorxiv.org/content/10.1101/2022.06.27.497673v2.
  • Jonathan B. Lynch§, Hsiao EY. Toward understanding links between the microbiome and neurotransmitters. Annals of the New York Academy of Sciences 1-7, 2023. -Highlighted in H1 Connect, 2023.
  • Jonathan B. Lynch§, James NG, McFall-Ngai M, Ruby EG, Shin S, Takagi D. Transitioning to confined spaces impacts bacterial swimming and escape response. Biophysical Journal 121(13), 2022. bioRxiv https://www.biorxiv.org/content/10.1101/2021.09.15.460467v1.
  • Jonathan B. Lynch, Bennett BD, Merrill BD, Ruby EG, Hryckowian AJ. A model symbiosis reveals host- and symbiont-derived phage protection mechanisms. Cell Reports 38(7), 2022. bioRxiv https://www.biorxiv.org/content/10.1101/2021.07.09.451802v1.
  • Vroom M, Rodruiguez-Ocasio Y, Jonathan B. Lynch, Ruby E, Foster J. Modeled microgravity alters lipopolysaccharide and outer membrane vesicle production of the beneficial symbiont Vibrio fischeri. npj Microgravity 7(8), 2021.
  • Cohen SK, Aschtgen M‐S, Jonathan B. Lynch, Koehler S, Chen F, Escrig S, Daraspe J, Ruby EG, Meibom A, McFall-Ngai M. Tracking the cargo of extracellular symbionts into host tissues with correlated electron microscopy and nanoscale secondary ion mass spectrometry imaging. Cellular Microbiology 22, 2020.
  • Jonathan B. Lynch§, Hsiao EY. Microbiomes as sources of emergent host phenotypes. Science, (365)6460, 2019. –Highlighted in Faculty Opinions, 2020
  • Schwartzman JA*, Jonathan B. Lynch*, Flores Ramos S, Zhou L, Apicella MA, Yew JY, Ruby EG. Acidic pH promotes lipopolysaccharide modification and alters colonization in a bacteria–animal mutualism. Molecular Microbiology, 112(4), 2019.
  • Jonathan B. Lynch, Schwartzman JA, Bennett BD, McAnulty SJ, Knop M, Nyholm SV, Ruby EG. Ambient pH Alters the Protein Content of Outer Membrane Vesicles, Driving Host Development in a Beneficial Symbiosis. Journal of Bacteriology, 201(20), 2019.
  • Jonathan B. Lynch§ and Alegado RA§. Spheres of hope, packets of doom: the good and bad of Outer Membrane Vesicles (OMVs) in interspecies and ecological dynamics. Journal of Bacteriology, 199(15), 2017.
  • Aschtgen MS, Jonathan B. Lynch, Koch E, Schwartzman J, McFall-Ngai M, Ruby E. Rotation of Vibrio fischeri flagella produces outer membrane vesicles that induce host development. Journal of Bacteriology 198(16), 2016.
  • Ng KM, Ferreyra JA, Higginbottom SK, Jonathan B. Lynch, Kashyap PC, Gopinath S, Naidu N, Choudhury B, Weimer BC, Monack DM, Sonnenburg JL. Microbiota-liberated host sugars facilitate post-antibiotic expansion of enteric pathogens. Nature 502(7469), 2013.
  • Jonathan B. Lynch and Sonnenburg JL. Prioritization of a plant polysaccharide over a mucus carbohydrate is enforced by a Bacteroides hybrid two-component system. Molecular Microbiology 85(3), 2012.
  • Harrison JE, Jonathan B. Lynch, Sierra LJ, Blackburn LA, Ray N, Collman RG, Doms RW. Baseline resistance of primary human immunodeficiency virus type 1 strains to the CXCR4 inhibitor AMD3100. Journal of Virology 82(23), 2008.

Stephen Gould, Ph.D.

Affiliation: Professor of Biological Chemistry

Description of Research

Research in the Gould lab is focused on the intersection of cell biology, bioengineering, and human disease.

Mechanisms of exosome biogenesis

Exosomes are small secreted vesicles of ~100 nm in size that play critical roles in human health and disease. We study the molecular mechanisms of exosome biogenesis by interrogating the biogenesis, intracellular trafficking, and vesicular secretion of highly enriched exosome cargo proteins, as well as viral proteins that use the hosts’ exosome biogenesis pathways for the formation of infectious viruses. Most recently, we’ve discovered that exosome marker proteins all bud primarily from the plasma membrane, and moreover, that endocytosis of exosome marker proteins from the plasma membrane greatly inhibits their vesicular secretion. These results re-write our understanding of exosome biogenesis by showing that it occurs primarily by direct budding from the plasma membrane, with only minor contributions from exocytosis of internal vesicles (Ai et al. Science Advances 2024, https://www.science.org/doi/10.1126/sciadv.adi9156).

Cell and exosome engineering

As the only bionormal nanovesicle, exosomes are an ideal delivery vehicle for vaccines, biologics, and drugs. Our laboratory uses our latest advances in exosome biogenesis to create proteins that are efficiently loaded into exosomes and confer unique properties on recombinantly engineered exosomes, including induction of immune responses, inhibition of angiogenesis, and other biomedically important activities. We then drive the high-level production of recombinant exosome-targeted proteins using new, highly restrictive antibiotic resistance genes that allow us to rapidly create cell lines that express the highest possible levels of recombinant proteins.

Synthetic signaling systems

Together with Dr. Michael Caterina’s lab, we’ve invented synthetic signaling systems that convert pathogenic signaling pathways into tunable, negative feedback loops that attenuate their pathogenic effects. These genetically-encoded tools are designed to ameliorate chronic diseases, with our primary focus on developing a safe and effective treatment for chronic pain.

Erin Goley, Ph.D.

Erin Goley, Ph.D.

Research Description

Bacteria are ubiquitous microorganisms that impact human health in myriad ways, including as pathogens and as commensal members of the microbiota. A fundamental understanding of the mechanisms of bacterial growth and adaptation is key to controlling their replication and survival. Our overarching research goal is to discover how bacteria grow, divide, and survive in diverse and potentially stressful environments. This is a particularly important goal as we confront the growing crisis in antimicrobial resistance.
Our laboratory takes a multi-faceted approach to study bacterial growth, incorporating cell biology, biochemistry, and genetic and genomic toolkits. We leverage two Gram-negative species: the free-living model Caulobacter crescentus and the obligate intracellular, tick-borne human pathogen Rickettsia parkeri. We take a comparative cell biology perspective to ask how growth, division, and adaptation of these two related bacteria has evolved to support survival in distinct growth environments.

NIH Bibliography page: https://www.ncbi.nlm.nih.gov/sites/myncbi/erin.goley.1/bibliography/50199813/public/

Current Lab Members

NameRole
Wanda Figueroa-Cuilan, PhDPostdoctoral Fellow
Erika SmithBCMB Graduate Student
Trung NguyenBCMB Graduate Student
Isaac PayneBCMB Graduate Student
Dezmond ColeBCMB Graduate Student

Publications (since joining Johns Hopkins)

Barrows JM, Anderson AS, Talavera-Figueroa BK and and Goley ED. (2023) Intrinsic and extrinsic factors regulate FtsZ function in Caulobacter crescentus. [pre-print] bioRxiv
Daitch AK and Goley ED. (2023) OpgH is an essential regulator of Caulobacter morphology. [pre-print] bioRxiv

Figueroa-Cuilan WM, Irazoki O, Feeley M, Smith E, Nguyen T, Cava F, Goley ED. (2023) Quantitative analysis of morphogenesis and growth dynamics in an obligate intracellular bacterium. MBoC. 34(7):ar69. (2023)

Barrows JM and Goley ED. (2023) Synchronized swarmers and sticky stalks: Caulobacter crescentus as a model for bacterial cell biology. J Bacteriology. e0038422.

Daitch AK, Orsburn BC, Chen Z, Alvarez L, Eberhard CD, Sundararajan K, Zeinert R, Kreitler DF, Jakoncic J, Chien P, Cava F, Gabelli SB, Goley ED. (2023) EstG is a novel esterase required for cell envelope integrity in Caulobacter. Current Biology. 33: 228-240. (2023)

Mahone CR, Yang X, McCausland JW, Payne IP, Xiao J, Goley ED. (2022) Integration of cell wall synthesis activation and chromosome segregation during cell division in Caulobacter. [pre-print] bioRxiv

Barrows JM and Goley ED. (2021) FtsZ dynamics in bacterial division: What, how, and why? Curr Opin Cell Biol. 68:163-172

Daitch AK and Goley ED. (2020) Uncovering unappreciated activities and niche functions of bacterial cell wall enzymes. Curr Biol. 30:R1170-R1175

Mahone CR and Goley ED. (2020) Bacterial Cell Division at a Glance. J Cell Science. 133: jcs237057 (2020)

Barrows JM*, Sundararajan K*, Bhargava A, Goley ED. (2020) FtsA Regulates Z-ring Morphology and Cell Wall Metabolism in an FtsZ C-terminal Linker Dependent Manner in C. crescentus. J Bacteriol. 202: e00693-19

Woldemeskel SA, Daitch AK, Alvarez L, Gaël Panis, Zeinert R, Gonzalez D, Smith E, Collier J, Chien P, Cava F, Viollier PH, Goley ED. (2020) The conserved transcriptional regulator CdnL is required for metabolic homeostasis and morphogenesis in Caulobacter. PLOS Genetics. 16: e1008591

Lariviere PJ, Mahone CR, Santiago-Collazo G, Howell M, Daitch AK, Zeinert R, Chien P, Brown PJB, Goley ED. (2019) An essential regulator of bacterial division links FtsZ to cell wall synthase activation. Current Biology. 29:1460-70

Howell ML, Aliaskevich A, Sundararajan K, Daniel JJ, Lariviere PJ, Goley ED, Cava F, Brown PJB. (2019) Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division. Mol Micro. 111:1074-92

Sundararajan K, Vecchiarelli AG, Mizuuchi K, Goley ED. (2018) Species- and C-terminal linker-dependent variations in the dynamic behavior of FtsZ on membranes in vitro. Mol Micro. 110: 47-63

Lambert A, Vanhecke A, Archetti A, Holden S, Schaber F, Pincus Z, Laub MT, Goley ED, and Manley S. (2018) Constriction rate modulation can drive cell size control and homeostasis in C. crescentus. iScience. 4: 180-189

Lariviere PJ, Szwedziak P, Mahone CR, Löwe J, and Goley ED. (2018) FzlA, an essential regulator of FtsZ protofilament curvature, controls constriction rate during Caulobacter division. Mol Micro. 107: 180-197.

Sundararajan K and Goley ED. (2017) The intrinsically disordered C-terminal linker of FtsZ regulates protofilament dynamics and superstructure in vitro. J Biol Chem. 292:20509-20527.

Meier EL, Yao Q, Daitch AK, Jensen GJ, and Goley ED. (2017) FtsEX-mediated regulation of the final stages of cell division reveals morphogenetic plasticity in Caulobacter crescentus. PLoS Genetics. 13:e1006999.

Woldemeskel SA, McQuillen R, Hessel AM, Xiao J, and Goley ED (2017) A conserved coiled-coil protein pair focuses the cytokinetic Z-ring in Caulobacter crescentus. Mol Micro. 105:721-740.

Woldemeskel SA and Goley ED (2017) Shapeshifting to survive: shape determination and regulation in Caulobacter crescentus. Trends Microbiol. 25:673-687.

Sundararajan K and Goley ED (2017) Cytoskeletal proteins in Caulobacter crescentus: spatial orchestrators of cell cycle progression, development, and cell shape. Subcell Biochem. 84:103-137.

Xiao J and Goley ED. (2016) Redefining the roles of the FtsZ-ring in bacterial cytokinesis. Curr Opin Microbiol. 34:90-96.

Meier EL, Ravazi S, Inoue T, and Goley ED. (2016) A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus. Mol Microbiol. 101:265-280.

Sundararajan K, Miguel A, Desmarais SM, Meier EL, Huang KC, and Goley ED. (2015) The bacterial tubulin FtsZ requires its intrinsically disordered linker to direct robust cell wall construction. Nat Commun. 6:7281.

Meier EL and Goley ED. (2014) Form and function of the bacterial cytokinetic ring. Curr Opin Cell Biol. 26:19-27.

Goley ED. (2013) Tiny cells meet big questions: a closer look at bacterial cell biology. Mol Biol Cell. 24:1099-102.

Ryuya Fukunaga, Ph.D.

Description of Research

Fukunaga lab investigates the mechanism and biology of post-transcriptional gene regulation controlled by RNA-binding proteins and small silencing RNAs. Our research projects will answer fundamental biological questions and also potentially lead to therapeutic applications to human disease.
For the RNA-binding proteins projects, we are interested in novel post-transcriptional gene regulation mechanism performed by uncharacterized or poorly characterized RNA-binding proteins. We use Drosophila oogenesis and spermatogenesis as one of the model systems since post-transcriptional gene regulation is particularly important during these processes.

For the small silencing RNA projects, we are particularly interested in the mechanisms by which microRNAs (miRNAs) and small interfering RNAs (siRNAs) are produced by Dicer enzymes and the mechanisms by the Dicer enzymes are regulated by Dicer-partner RNA-binding proteins. Specifically, we aim to understand the molecular mechanism by which the length of small silencing RNAs produced by Dicer is defined and regulated, which is a biologically significant question.

We use a combination of biochemistry, biophysics, Drosophila genetics, cell culture, and next-generation sequencing, in order to understand important biological questions from the atomic to the organismal level.

Lab Members

  • Azali Azlan (postdoc)
  • Yuki Taira (postdoc)

Publications

  • Zhu L, Fukunaga R. RNA-binding protein Maca is crucial for gigantic male fertility factor gene expression, spermatogenesis, and male fertility, in Drosophila. PLoS Genetics. 17, e1009655, (2021)
  • Vakrou S, Liu Y, Zhu L, Greenland GV, Simsek B, Hebl BV, Guan Y, Woldemichael K, Talbot CC, Aon MA, Fukunaga R, Abraham MR. Differences in molecular phenotype in mouse and human hypertrophic cardiomyopathy. Scientific Reports. 11, 13163, (2021)
  • Liu Y, Afzal J, Vakrou S, Greenland GV, Talbot CC Jr, Hebl VB, Guan Y, Karmali R, Tardiff JC, Leinwand LA, Olgin JE, Das S, Fukunaga R, Abraham MR. Differences in microRNA-29 and Pro-fibrotic Gene Expression in Mouse and Human Hypertrophic Cardiomyopathy. Front Cardiovasc Med. 6,170, (2019)
  • Zhu L, Liao ES, Fukunaga R. Drosophila Regnase-1 RNase is required for mRNA and miRNA profile remodelling during larva-to-adult metamorphosis. RNA Biology 16, 1386-1400, (2019)
  • Zhu L, Liao ES, Ai Y, Fukunaga R. RNA methyltransferase BCDIN3D is crucial for female fertility and miRNA and mRNA profiles in Drosophila ovaries. PLoS ONE 14, e0217603, (2019)
  • Liao ES, Kandasamy SK, Zhu L, Fukunaga R. DEAD-box RNA helicase Belle post-transcriptionally promotes gene expression in an ATPase activity-dependent manner. RNA 25, 825-839, (2019)
  • Zhu L, Kandasamy SK, Liao ES, Fukunaga R. LOTUS domain protein MARF1 binds CCR4-NOT deadenylase complex to post-transcriptionally regulate gene expression in oocytes. Nature Communications, 9, 4031, (2018)
  • Liao ES, Ai Y, Fukunaga R. An RNA-binding protein Blanks plays important roles in defining small RNA and mRNA profiles in Drosophila testes. Heliyon, 4, e00706, (2018)
  • Vakrou S, Fukunaga R, Foster DB, Sorensen L, Liu Y, Guan Y, Woldemichael K, Pineda-Reyes R, Liu T, Jill C. Tardiff JC, Leinwand LA, Tocchetti CG, Abraham TP, Brian O’Rourke B, Aon MA, Abraham MR. Allele-specific differences in transcriptome, miRNome, and mitochondrial function in two hypertrophic cardiomyopathy mouse models. JCI insight, 3, e94493, (2018)
  • Fukunaga R. Dicer-2 partner protein Loquacious-PD allows hairpin RNA processing into siRNAs in the presence of inorganic phosphate. Biochemical and Biophysical Research Communications, 498, 1022–1027, (2018)
  • Zhu L, Kandasamy SK, Fukunaga R. Dicer partner protein tunes the length of miRNAs using base-mismatch in the pre-miRNA stem. Nucleic Acids Res., 46, 3726-3741, (2018)
  • Kandasamy SK, Zhu L, Fukunaga R. The C-terminal dsRNA-binding domain of Drosophila Dicer-2 is crucial for efficient and high-fidelity production of siRNA and loading of siRNA to Argonaute2. RNA, 23, 1139-1153, (2017)
  • Kandasamy SK, Fukunaga R. Phosphate-binding pocket in Dicer-2 PAZ domain for high-fidelity siRNA production. Proc. Natl. Acad. Sci. U S A. 113, 14031-14036, (2016)
  • Lin X, Steinberg S, Kandasamy S, Afzal J, Mbiyangandu B, Liao ES, Guan Y, Corona-Villalobos C, Matkovich S, Epstein N, Tripodi D, Huo Z, Cutting G, Abraham T, Fukunaga R, Abraham R. Common MiR-590 Variant rs6971711 present only in African Americans reduces miR-590 biogenesis. PLoS ONE. 11, e0156065, (2016)
  • Yanagisawa T, Ishii R, Hikida Y, Fukunaga R, Sengoku T, Sekine SI, Yokoyama S. A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys. J. Struct. Funct. Genomics. 16, 25-41, (2015)
  • Fukunaga R, Colpan C, Han BW, Zamore PD. Inorganic phosphate blocks binding of pre-miRNA to Dicer-2 via its PAZ domain. EMBO Journal, 18, 371-384, (2014)
  • Fukunaga R, Han BW, Hung JH, Xu J, Weng Z, Zamore PD. Dicer Partner Proteins Tune the Length of Mature miRNAs in Flies and Mammals. Cell, 151, 533-546, (2012)
  • Cenik ES, Fukunaga R, Lu G, Dutcher R, Wang Y, Tanaka Hall TM, Zamore PD. Phosphate and R2D2 Restrict the Substrate Specificity of Dicer-2, an ATP-Driven Ribonuclease. Mol. Cell, 42, 172-814, (2011)
  • Naganuma M, Sekine SI, Fukunaga R, Yokoyama S. Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization. Proc. Natl. Acad. Sci., 106, 8489-8494, (2009)
  • Fukunaga R, Doudna JA. dsRNA with 5¢ overhangs contributes to endogenous and antiviral RNA silencing pathways in plants. EMBO J., 28, 545-555, (2009)
  • Yanagisawa T, Ishii R, Fukunaga R, Kobayashi T, Sakamoto K, Yokoyama S. Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N¢-(o-Azidobenzyloxycarbonyl) lysine for site-specific protein modification. Chem. Biol., 15, 1187-1197, (2008)
  • Fukunaga R, Harada Y, Hirao I, Yokoyama S. Phosphoserine aminoacylation of tRNA bearing an unnatural base anticodon. Biochem Biophys Res Commun., 372, 480-485, (2008)
  • Yanagisawa T, Ishii R, Fukunaga R, Kobayashi T, Sakamoto K, Yokoyama S. Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase. J. Mol. Biol., 378, 634-652, (2008)
  • Fukunaga R, Yokoyama S. Structural insights into the second step of RNA-dependent cysteine biosynthesis in archaea: crystal structure of Sep-tRNA:Cys-tRNA synthase from Archaeoglobus fulgidus. J. Mol. Biol., 370, 128-141, (2007)
  • Fukunaga R, Yokoyama S. The C-terminal domain of the archaeal leucyl-tRNA synthetase prevents misediting of isoleucyl-tRNAIle. Biochemistry, 46, 4985-4996, (2007)
  • Fukunaga R, Yokoyama S. Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Nat. Struct. Mol. Biol., 14, 272-279, (2007)
  • Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus. Acta Crystallogr. F, 63, 224-228, (2007)
  • Fukunaga R, Yokoyama S. Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii. Acta Crystallogr. D, 63, 390-400, (2007)
  • Yanagisawa T, Ishii R, Fukunaga R, Nureki O, Yokoyama S. Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the Methanogenic archaeon Methanosarcina mazei. Acta Crystallogr. F, 62, 1031-1033, (2006)
  • Sasaki H, Sekine S, Sengoku T, Fukunaga R, Hattori M, Utsunomiya Y, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S. Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase. Proc. Natl. Acad. Sci. 103, 14744-14749, (2006)
  • Fukunaga R, Yokoyama S. Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase. J. Mol. Biol. 359, 901-912, (2006)
  • Kuratani M, Ishii R, Bessho Y, Fukunaga R, Sengoku T, Sekine S, Shirouzu M, Yokoyama S. Crystal structure of tRNA adenosine deaminase TadA from Aquifex aeolicus. J. Biol. Chem., 280, 16002-16008, (2005)
  • Tukalo M, Yaremchuk A, Fukunaga R, Yokoyama S, Cusack S. The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nat. Struct. Mol. Biol. 12, 923-930, (2005)
  • Fukunaga R, Yokoyama S. Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator base recognition for 3¢-end relocation toward the editing domain. Nat. Struct. Mol. Biol. 12, 915-922, (2005)
  • Fukunaga R, Yokoyama S. Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain. J. Biol. Chem. 280, 29937-29945, (2005)
  • Fukunaga R, Ishitani R, Nureki O, Yokoyama S. Crystallization of Leucyl-tRNA synthetase complexed with tRNALeu from the archaeon Pyrococcus horikoshii. Acta Crystallogr. F, 61, 30-32, (2005).
  • Fukunaga R, Yokoyama S. Crystal Structure of Leucyl-tRNA Synthetase from the Archaeon Pyrococcus horikoshii Reveals a novel editing domain orientation. J. Mol. Biol. 346, 57-71, (2005).
  • Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii. Acta Crystallogr. D, 60, 1916-1918, (2004)
  • Fukunaga R, Yokoyama S. Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues. Acta Crystallogr. D, 60, 1900-1902, (2004)
  • Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S. Crystal Structures of the CP1 Domain from Thermus thermophilus Isoleucyl-tRNA synthetase and Its Complex with L-Valine. J. Biol. Chem. 279, 8396-8402, (2004)
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