Research Topics
Genomes and Genes | Murray StewartSummaryAffiliation: University of Cambridge Country: UK Publications
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Publications
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein importM Stewart
MRC Laboratory of Molecular Biology, Hills Rd, CB2 2QH, Cambridge, UK
FEBS Lett 498:145-9. 2001....- Structural biology. Nuclear traffickingMurray Stewart
MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UK
Science 302:1513-4. 2003 - Molecular mechanism of the nuclear protein import cycleMurray Stewart
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Nat Rev Mol Cell Biol 8:195-208. 2007.... - Insights into the molecular mechanism of nuclear trafficking using nuclear transport factor 2 (NTF2)M Stewart
Medical Research Council Laboratory of Molecular Biology, Cambridge, England
Cell Struct Funct 25:217-25. 2000..An analogous nucleoporin hopping mechanism may also be used by carrier molecules of the importin-beta family to move through NPCs... - Ratcheting mRNA out of the nucleusMurray Stewart
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK
Mol Cell 25:327-30. 2007..In budding yeast, recent work suggests that the DEAD-box helicase Dbp5 remodels mRNPs at the NPC cytoplasmic face by removing Mex67 and that the Dbp5 ATPase is activated by Gle1 and inositol hexaphosphate (IP(6))... - 1.9 A resolution crystal structure of the Saccharomyces cerevisiae Ran-binding protein Mog1pM Stewart
MRC Laboratory of Molecular Biology, Cambridge, England
J Mol Biol 299:213-23. 2000.... - Structural basis for the nuclear protein import cycleM Stewart
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Biochem Soc Trans 34:701-4. 2006..Interactions between transport factors and key nucleoporins (such as Nup1p, Nup2p and Nup50) accelerate the formation and dissolution of many of these complexes... - Nuclear pores and macromolecular assemblies involved in nucleocytoplasmic transportM Stewart
MRC Laboratory of Molecular Biology, Cambridge, UK
Curr Opin Struct Biol 6:162-5. 1996..In addition to NPC-based complexes, such as those based on nucleoporins Nsp1p and p62, cytoplasmic protein macromolecular assemblies are also important for nucleocytoplasmic transport... 
Nuclear export of mRNAMurray Stewart
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 0QH, UK
Trends Biochem Sci 35:609-17. 2010..Recent structural and cell biology results provide key information that should enable development of a detailed understanding of this central cellular process at a molecular level...
Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1Andrew M Ellisdon
From the Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom and
J Biol Chem 285:3850-6. 2010..Biol. Chem. 284, 12049-12056). A single Sus1 molecule cannot bind Sgf11 and Sac3 simultaneously and this, combined with the structure of the Sus1-Sgf11 complex, indicates that Sus1 forms separate subcomplexes within SAGA and TREX-2...- Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complexAndrew M Ellisdon
Medical Research Council Laboratory of Molecular Biology, Cambridge, UK
Nat Struct Mol Biol 19:328-36. 2012.... - Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2Richard P Grant
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
J Mol Biol 376:1048-59. 2008.... - Structural basis for the assembly of a nuclear export complexYoshiyuki Matsuura
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Nature 432:872-7. 2004.... - Structural basis for the function of the Saccharomyces cerevisiae Gfd1 protein in mRNA nuclear exportChao Zheng
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom
J Biol Chem 285:20704-15. 2010..These data support the importance of the Gfd1/Nab2 interaction for Dbp5 activity and provide further molecular details of the interactions that facilitate Dbp5-mediated mRNP remodeling in the terminal step of mRNA export... - Functional and structural characterization of the mammalian TREX-2 complex that links transcription with nuclear messenger RNA exportDivyang Jani
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Nucleic Acids Res 40:4562-73. 2012..Thus, we implicate TREX-2 as an integral component of the mammalian mRNA export machinery where it links transcription and nuclear export by facilitating the transfer of mature mRNPs from the nuclear interior to NPCs... - Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeatsJonathan Morrison
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
J Mol Biol 333:587-603. 2003.... - Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95pSai Man Liu
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
J Mol Biol 349:515-25. 2005..The length and composition of this linker is crucial and suggests how differences in affinity for Kap95p both between and within FG-nucleoporins arise... - Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its function in mRNA nuclear exportChristoph Brockmann
Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK
Structure 20:1007-18. 2012.... - Structural basis for nuclear import complex dissociation by RanGTPSoo Jae Lee
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, UK
Nature 435:693-6. 2005..This interaction produces a change in helicoidal pitch that locks Kap95p in a conformation that cannot bind importin-alpha or cargo. We suggest an allosteric mechanism for nuclear import complex disassembly by RanGTP... - Structural basis for the interaction between NTF2 and nucleoporin FxFG repeatsRichard Bayliss
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
EMBO J 21:2843-53. 2002.... - Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear traffickingR Bayliss
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom
Cell 102:99-108. 2000..Instead, RanGTP may release importin-beta from FxFG nucleoporins by generating a conformational change that alters the structure of the FxFG binding site... - Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA exportDivyang Jani
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Mol Cell 33:727-37. 2009..These data indicate Sac3(CID) provides a scaffold within TREX-2 to integrate interactions between protein complexes to facilitate the coupling of transcription and mRNA export during gene expression... - Novel binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-alphaAstrid Giesecke
Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom
J Biol Chem 285:17628-35. 2010..The different way in which TPX2 binds to importin-alpha could account for much of the selectivity necessary during mitosis because this would reduce the competition for binding to importin-alpha from other NLS-containing proteins... - GLFG and FxFG nucleoporins bind to overlapping sites on importin-betaRichard Bayliss
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom
J Biol Chem 277:50597-606. 2002..The binding of GLFG and FxFG repeats to overlapping sites on importin-beta indicates that functional differences between different repeats probably arise from differences in their spatial organization... - Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear importYoshiyuki Matsuura
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
EMBO J 22:5358-69. 2003..These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process... - Nup50/Npap60 function in nuclear protein import complex disassembly and importin recyclingYoshiyuki Matsuura
MRC Laboratory of Molecular Biology, Cambridge, UK
EMBO J 24:3681-9. 2005..These results provide a rationale for understanding the series of interactions that orchestrate the terminal steps of nuclear protein import... - Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolutionRichard P Grant
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
J Mol Biol 326:849-58. 2003.... - Nuclear protein import is decreased by engineered mutants of nuclear transport factor 2 (NTF2) that do not bind GDP-RanW D Clarkson
MRC Laboratory of Molecular Biology, Cambridge, UK
J Mol Biol 272:716-30. 1997..We conclude that interaction between NTF2 and GDP-Ran is important for efficient nuclear protein import... - Molecular interactions between the importin alpha/beta heterodimer and proteins involved in vertebrate nuclear protein importP Percipalle
MRC Laboratory of Molecular Biology, Cambridge, England
J Mol Biol 266:722-32. 1997..Our results are consistent with models for nuclear protein import in which Ran nucleotide exchange modulates the binding of the importin-substrate complexes during translocation through nuclear pore complexes... - The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)T L Bullock
MRC Laboratory of Molecular Biology, Cambridge, UK
J Mol Biol 260:422-31. 1996.... - Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase RanM Stewart
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, England
J Mol Biol 277:635-46. 1998..The binding of GDP-Ran at the NTF2 cavity raises the possibility that this interaction might be modulated by a metabolite or small molecule substrate for NTF2's putative enzymatic activity... - GANP enhances the efficiency of mRNA nuclear export in mammalian cellsVihandha O Wickramasinghe
MRC Cancer Cell Unit, Hutchison MRC Research Centre, Cambridge, UK
Nucleus 1:393-6. 2010..Here, we discuss the model for GANP function presented in our recent paper and its implications for the mechanism of mRNA export in mammalian cells... - Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motilityRichard P Grant
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, UK
J Mol Biol 347:583-95. 2005..This observation, together with the structural data, suggests that MFP2 may function in a manner analogous to formins in actin-based motility... - Structural basis for the nuclear import of the human androgen receptorMark L Cutress
Uro Oncology Research Group, Cancer Research UK Cambridge Research Institute, Robinson Way, Cambridge, CB2 0RE, UK
J Cell Sci 121:957-68. 2008..Thus, in addition to its function in the nuclear import of AR, the NLS in the hinge region of AR has a separate, quite distinct role on transactivation, which becomes apparent once nuclear import has been achieved... - mRNA export from mammalian cell nuclei is dependent on GANPVihandha O Wickramasinghe
MRC Cancer Cell Unit, Hutchison MRC Research Centre, Hills Road, Cambridge CB2 0XZ, UK
Curr Biol 20:25-31. 2010..These results establish GANP as an integral component of the mammalian mRNA export machinery and suggest a model whereby GANP facilitates the transfer of NXF1-containing mRNPs to NPCs... - NTF2 monomer-dimer equilibriumC Chaillan-Huntington
Laboratory of Molecular Biology, MRC, Hills Road, Cambridge, CB2 2QH, England
J Mol Biol 314:465-77. 2001..Overall, our results indicate that dimer formation is important for NTF2 function and give insight into the formation of heterodimers by mRNA export factors such as TAP1 and NXT1 that contain NTF2-homology domains... - Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1Richard P Grant
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
Nat Struct Biol 9:247-51. 2002..F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function... - Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargoAbigail M Fox
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom
J Biol Chem 286:29325-35. 2011.... - Interaction between Ran and Mog1 is required for efficient nuclear protein importR P Baker
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom
J Biol Chem 276:41255-62. 2001..Our results indicate that a primary function of Mog1 requires binding to Ran and that the Mog1-Ran interaction is necessary for efficient nuclear protein import in vivo... - Cytoskeleton dynamics powers nematode sperm motilityMurray Stewart
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, England
Adv Protein Chem 71:383-99. 2005..Overall, nematode sperm motility illustrates that cell locomotion can be generated by cytoskeletal dynamics alone without the use of myosin-like motor proteins... - Crystallization and preliminary X-ray diffraction analysis of nuclear transport factor 2H M Kent
MRC Laboratory of Molecular Biology, Cambridge, England
J Struct Biol 116:326-9. 1996..9 A; b = 56.7 A; c = 88.3 A and diffract past 2 A on laboratory X-ray sources. The asymmetric unit of these crystals contains two NTF2 polypeptide chains, consistent with the reported dimeric structure of the molecule... - The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2)M Stewart
MRC Laboratory of Molecular Biology, Hills Rd, Cambridge, CB2 2QH
J Mol Biol 284:1517-27. 1998..This interaction between NTF2 and GDP-Ran is required for efficient nuclear protein import and may function between the docking and translocation steps of the pathway... - 2.6 A resolution crystal structure of helices of the motile major sperm protein (MSP) of Caenorhabditis elegansAnne M E Baker
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK
J Mol Biol 319:491-9. 2002..The interfaces frequently involve the loop containing residues 78-85, which is divergent between MSP homologues, and the loop containing residues 98-103, which is highly conserved... - Crystallization and preliminary X-ray diffraction analysis of the Saccharomyces cerevisiae ran-binding protein Mog1pR P Baker
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England
Acta Crystallogr D Biol Crystallogr 56:229-31. 2000..The crystals have P2(1)2(1)2(1) symmetry, with unit-cell parameters a = 39.67, b = 51.96, c = 112.23 A, a Matthews coefficient of 2.44 A(3) Da(-1), an estimated solvent content of 49.5% and one chain in the asymmetric unit... 
Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62F Buss
Medical Research Council Laboratory of Molecular Biology, Cambridge, England
J Cell Biol 128:251-61. 1995..This model is consistent with data that indicate that the analogous coiled-coil region of yeast nucleoporin NSP1 may function in a similar way...- The molecular mechanism of translocation through the nuclear pore complex is highly conservedCarl Feldherr
Department of Anatomy and Cell Biology, University of Florida, College of Medicine, Gainesville 32610, USA
J Cell Sci 115:2997-3005. 2002..Since selected nuclear import pathways can be investigated in the absence of competing endogenous transport, A. proteus might provide a useful in vivo system for investigating specific molecular interactions involved in trafficking... - Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound conformation: implications for nuclear import complex assembly dynamicsJade K Forwood
School of Biomedical Sciences, Charles Sturt University, Wagga Wagga 2650, Australia
J Mol Biol 383:772-82. 2008..The structure of the complex provides insights into the structural basis for the gradation of affinities regulating nuclear protein transport... - Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-TKenji Murakami
Department of Biosciences, School of Science and Engineering, Teikyo University, Toyosatodai 1 1, Utsunomiya 320 8551, Japan
Proc Natl Acad Sci U S A 105:7200-5. 2008..On actin filaments, the head-to-tail junction can function as a molecular swivel to accommodate irregularities in the coiled-coil path between successive tropomyosins enabling each to interact equivalently with the actin helix... - Coordination of Hpr1 and ubiquitin binding by the UBA domain of the mRNA export factor Mex67Maria Hobeika
Institut Jacques Monod, Universités Paris VI and VII, Centre National de la Recherche Scientifique, 75251 Paris Cedex 05, France
Mol Biol Cell 18:2561-8. 2007.... - Classical nuclear localization signals: definition, function, and interaction with importin alphaAllison Lange
Department of Biochemistry, School of Medicine, Emory University, Atlanta, Georgia 30322, USA
J Biol Chem 282:5101-5. 2007..Finally, we describe how a predicted NLS within a protein of interest can be confirmed experimentally to be functionally important... - Karyopherin flexibility in nucleocytoplasmic transportElena Conti
EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany
Curr Opin Struct Biol 16:237-44. 2006..Flexibility appears to be an intrinsic feature of such superhelices and might be functionally important not only for karyopherins and nuclear transport, but also for HEAT repeat proteins from other biological systems... - Meeting report: International Symposium on 'Ran and the Cell Cycle', October 2-5, 2005, Awaji Yumebutai, JapanMary Dasso
Laboratory of Gene Regulation and Development, NICHD, NIH, Bethesda, MD 20892-5431, USA
Traffic 7:474-8. 2006 - Structural basis for vertebrate filamin dimerizationRegina Pudas
Biocenter Oulu and Department of Biochemistry, University of Oulu, Finland
Structure 13:111-9. 2005..Furthermore, we show that point mutations in the dimerization interface disrupt the dimer and that the dissociation constant for recombinant Ig24 is in the micromolar range... - Functional significance of the interaction between the mRNA-binding protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA exportMilo B Fasken
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA
J Biol Chem 283:27130-43. 2008..These data provide in vivo evidence for a model of mRNA export in which Nab2 is important for targeting mRNAs to the nuclear pore for export...