EMBL Australia Showcase
EMBL Australia ShowcaseTuesday 5th July 2016EMBL Australia acknowledges the support of The John CurtinSchool of Medical Research and Australian National University insponsoring the 2016 EMBL Australia Showcase.
European Molecular BiologyLaboratory AustraliaWhat isEMBL Australia?Buildinginternational linksEmpowering youngresearchersEmbeddingbioinformatics inAustralian life sciencePromoting systemsbiologyEMBL Australia is a life sciencenetwork that supports researchprojects and provides infrastructureand training.It was created in 2008 to maximisethe benefits of Australia’s associatemembership of the EuropeanMolecular Biology Laboratory (EMBL).EMBL Australia is jointly run byUniversities Australia, the Associationof Australian Medical ResearchInstitutes, CSIRO and BioplatformsAustralia.“EMBL Australia has created a uniqueadvantage for emerging Australianscientific talent with an enriched andsustainable international collaborativeframework which positions Australiandiscoveries in the spotlight andoffers our scientists access to anextraordinarily valuable professionalknowledge network.”Professor Brandon Wainwright,Chair, EMBL Australia CouncilAbout EMBL—Europe’slife science flagshipThe European Molecular BiologyLaboratory was founded in 1974, whenthe field was strongly dominated by theUnited States.Its 20 member states realised thattogether they could compete andachieve more than each could bythemselves.With nodes in the UK (Hinxton, nearCambridge), France (Grenoble),Germany (Heidelberg and Hamburg)and Italy (Monterotondo, near Rome),EMBL now comprises about85 independent research groupsand more than 1,400 people.Among its many features are: nine years of funding securityfor research leaders (subject toperformance), after which theymove on training for young researchers—over 3,000 per year highly-sought post-doctoral positions research networks across Europeand around the world a culture that focuses on youngscientists and builds strongresearch alliances.In 2008, Australia became EMBL’s firstAssociate Member State.
Tuesday 5th July 2016Program9.10amIntroduction, Thomas Preiss9.15amWelcome Address, Simon Foote, Director, John Curtin School of Medical Research9.20amMatthias Hentze – A new view on RNA-binding proteins and RNA9.50amVille-Petteri Makinen – Integrative genomics and network biology of commonchronic diseases10.20amMax Cryle – Understanding Glycopeptide Antibiotic biosynthesis as a pathway to newantimicrobial agents10.50amBreak11.15amMate Biro – The actin cortex at the interface of cancer and immunity: T cell migrationand cytotoxic interactions11.45amMirana Ramialison – From regulatory elements to cardiac enhanceropathies12.15pmPresentation by Matthias Hentze to new EMBL Australia Collaborating GroupLeader, Mirana Ramialison12.25pmLunch1.10pmMichael Parker – Cholesterol-dependent cytolysins: from water-soluble state tomembrane pore1.40pmEdwina McGlinn – Regulation of Hox cluster dynamics during development2.10pmAndrew Lonie – Building the EMBL Australia Bioinformatics Resource2.40pmBreak2.55pmDavid Lynn – The impact of the neonatal microbiome on specific and non-specificvaccine responses3.25pmChen Davidovich – Mechanism of RNA binding by the Polycomb repressivecomplex 2 (PRC2)3.55pmThomas Preiss – Dynamics of ribosome scanning and recycling revealed by translationcomplex profiling4.25pmFinish
Speaker BiosVille-Petteri MäkinenEMBL Australia Group Leader,South Australia Health andMedical Research InstituteVille-Petteri Mäkinen holds an EMBLAustralia Group Leader positionwithin the Heart Health Theme inthe South Australian Health andMedical Research Institute, andaffiliate professorship in the School ofMolecular and Biomedical Science atthe University of Adelaide. He is alsoa part-time Senior Research Fellowin Computational Medicine in theInstitute of Health Sciences in Oulu,Finland. Mäkinen’s research focuseson the molecular features of metabolicdysfunction in human populations andthe genetic causes that increase therisk of diabetes, atherosclerosis anddementia in vulnerable subgroups. Hehas published several key findings inthe field, particularly related to type 1diabetes and metabolic phenotypingof diabetic nephropathy, and heis determined to develop networkand systems biology approaches toelucidate the pathogenic processesthat predispose young individualsto chronic morbidity later in life.Moreover, he is actively developingnovel study designs to improve thematch between the findings in animalmodels and the correspondingphenomena in human cohorts.Integrative genomics and networkbiology of common chronicdiseases”Aging and sedentary life style drive the current worlwide epidemicsof obesity, diabetes, heart disease and dementia. The complexetiology and the tendency to co-occur in vulnerable individualsmake it difficult to investigate the specific molecular pathways orenvironmental risk factors of these progressive chronic conditionsin detail. Omics technologies and network biology have openednew ways of collecting vast amount of molecular information andthere is great potential in translating the data into preventative andcurative approaches in public health and clinical practice. However,the complex and overlapping nature of these data does not fit wellwith the traditional reductionist approaches that still dominate thegeneration of wet lab hypothesis and testing in animal models. In thistalk, I will provide examples of our work in defining human phenotypesthat convey a high risk of disease, how to integrate cross-speciesmulti-omics datasets, and I will also discuss new ways to createcoherent research projects that span the gap between epidemiologyand experimental validation in vivo in the era of big data.
Edwina McGlinnEMBL Australia Group Leader,Australian RegenerativeMedicine Institute, MonashUniversityEdwina McGlinn is an EMBL- AustraliaPartner Network Lab Group Leader,based at the Australian RegenerativeMedicine Institute, Monash University.Edwina’s research focuses ondeciphering genetic networks duringearly embryonic development, withparticular emphasis on microRNAcontrol of Hox gene networks. Edwinacompleted a PhD in developmentaland molecular biology at theInstitute for Molecular BioscienceUQ, identifying novel downstreameffectors of Sonic hedgehog in thedeveloping mouse limb. She thenbecame a research fellow in thelaboratory of Professor CliffordTabin, Harvard Medical School USA,dissecting genetic networks involvedin patterning the vertebrate limb andaxial skeleton.Regulation of Hox cluster dynamicsduring development”Hox gene regulatory networks are critical in the development of almostevery mammalian organ system, providing the positional informationnecessary for region appropriate identity and function. This importanceextends to regulatory mechanisms that contribute to refining orstabilising Hox expression. The identification of numerous microRNAsthat are not only embedded within Hox clusters, but also targetnumerous Hox genes, suggests an important role for these regulatorymolecules in shaping Hox protein output. Here, we use an extensiveallelic series of mouse knock-in/knockouts to address the functionof a Hox-embedded microRNA family (miR-196) within Hox genenetworks. We demonstrate that miR-196 has the ability to regulatethe correct temporal progression of Hox gene activation from all fourHox clusters, with specific focus on how this impacts formation of thevertebral column and neural networks of the spinal cord.
Speaker BiosDavid LynnEMBL Australia Group Leader,Infection & Immunity, SAHMRIDavid is an EMBL Australia Group Leaderin the Infection and Immunity Theme atthe South Australian Health and MedicalResearch Institute (SAHMRI). He alsoholds a joint faculty appointment asAssociate Professor at the School ofMedicine, Flinders University. Davidheads a multi-disciplinary group that isequally divided between bioinformaticsand experimental systems biology. Onthe wet-lab side, his group employs invitro and in vivo experimental and clinicalmodels coupled with systems biologyapproaches to investigate the interplaybetween the microbiome, vaccines andthe immune system. On the bioinformaticsside, his group leads the developmentof InnateDB.com, an internationallyrecognised systems biology platform forinnate immunity networks and he alsoleads the computational biology aspectsof 12 million European Commissionfunded project called PRIMES, whichis investigating how to model andsubsequently therapeutically target proteininteraction networks in cancer.His Group is currently supportedby: EMBL Australia, The EuropeanCommission, NHMRC, and The GarnettPasse and Rodney Williams MemorialFoundation. He has attracted 5 millionin funding in the last 5 years. He haspublished 50 papers in journals includingScience, Science Translational Medicine,Molecular Systems Biology, Journal ofInfectious Diseases and his publicationshave received more than 3,400 citations.He has given invited talks on 6 continents.The impact of the neonatalmicrobiome on specific andnon-specific vaccine responses”In their first months of life, infants worldwide receive vaccinationsproviding protection against many serious infectious diseases.However, vaccine efficacy varies substantially among individualsand clinical trials show consistently lower vaccine immunogenicity indeveloping world populations. One potential, but poorly considered,contributor to this variation is the intestinal microbiome. The gut hostsan enormous abundance and diversity of microbes, which performa range of essential and beneficial functions. In neonates, the gutmicrobiome is rapidly established and, in vaginally-born infants, itscomposition is strongly determined by the maternal microbiome.However, up to 40% of neonates are exposed to antibiotics, eitherdirectly or maternally, during the perinatal period and this has beendocumented to lead to a dysregulation of the normal development ofthe microbiome, causing dysbiosis. It is increasingly well-establishedthat the consequences of dysbiosis can be long-lasting and extendfar beyond the gut, leading to a dysregulation of systemic metabolismand immunity. We hypothesise that antibiotic-induced intestinaldysbiosis, particularly in this critical neonatal period, could lead toimpaired immune responses to routine infant immunisations, whichcommence in close proximity to perinatal antibiotic exposure. We havenow proven this to be the case in a neonatal mouse model, wherewe have demonstrated significant impairment of antigen-specificresponses to three different routinely-administered infant vaccines.
Maté BiroEMBL Australia New SouthWales NodeSingle Molecule Science andARC Centre of Excellence inAdvanced Molecular Imaging,University of New South Wales,Sydney, AustraliaMaté Biro received his PhD at theMax Planck Institute of Molecular CellBiology and Genetics in Germany in2011. His doctoral work focused onthe biophysics of cellular actin cortexassembly. He previously studiedPhysics (BSc) and then Bioinformaticsand Theoretical Systems Biology (MSc)at the Imperial College in London, UK,and did his Masters research at MIT,Cambridge, MA, USA. He has workedat a particle accelerator in Tsukuba,Japan and as a Research Associateat the Bioinformatics Institute of theA*STAR in Singapore. In 2012, hemoved to Sydney and the CentenaryInstitute at the University of Sydney,where he initially worked as a postdocand then as of 2014 as group leaderof the Cellular Mechanobiology lab.Maté joined EMBL Australia as a groupleader at Single Molecule Sciencenode at UNSW in January 2016. Hisresearch, highly multidisciplinary innature, focuses on the dynamics andregulation of the actin cytoskeleton,notably during the migration ofT cells and tumour cells, and theimmunological interactionsbetween them.The actin cortex at the interfaceof cancer and immunity: T cellmigration and cytotoxic interactions”The cellular actin cortex is the cytoskeletal structure primarilyresponsible for the control of animal cell shape and as such plays acentral role in cell migration. In adaptive immune responses to solidcancers, and in burgeoning adoptive transfer immunotherapies,T cells need to navigate various barriers and organs to reach thetumour and then effectively find and engage their targets. Thesetypes of tissue-invasive cell migrations and interactions rely onpolarised shape changes and forces mediated by the actomyosincortex, which manifest in different cellular protrusions, such aslamellipodia, filopodia and blebs, whose functional significance remainincompletely understood. We develop and adapt novel tools toresolve the composition, dynamics and regulation of the cell cortexand protrusions in motility and cytotoxic interactions, based on anintegrative and multidisciplinary method encompassing microscopy,innovative image analysis, biophysical manipulation and computationalmodelling. We aim to uncover the cytoskeletal mechanisms thatunderpin effective target scanning by cytotoxic T cells, as well as theirtumour rejection potential.
Speaker BiosThomas PreissEMBL – Australia CollaboratingGroup LeaderDepartment of GenomeSciences, The John CurtinSchool of Medical Research,The Australian NationalUniversityThomas Preiss is Professor of RNABiology at The Australian NationalUniversity (ANU). From 1986–91he studied Chemistry in Marburg(Germany) and Bristol (UK). He joinedthe field of RNA research with hisPhD (1992–95) in Newcastle uponTyne (UK) and postdoctoral training(1995–2002) at the EMBL, Heidelberg(Germany). In 2002 he moved to theVCCRI in Sydney. At ANU since 2011,his lab focuses on the mechanismsof mRNA utilisation and its regulationby RNA-binding proteins, RNAmodifications and non-coding RNAs.He studies these phenomena in thecontexts of cardiac disease, stem cellbiology and cancer.Dynamics of ribosome scanningand recycling revealed by translationcomplex profiling”Regulation of mRNA translation is central to eukaryotic gene expressioncontrol. Regulatory inputs are specified by the mRNA untranslatedregions (UTRs) and often target translation initiation. Initiation involvesbinding of the 40S ribosomal small subunit (SSU) and associatedinitiation factors (eIFs) near the mRNA 5’ cap; the SSU then ‘scans’ inthe 3’ direction until it detects the start codon and is joined by the 60Sribosomal large subunit (LSU) to form the 80S ribosome (RS). Scanningand other dynamic aspects of the initiation model remain conjectureas methods to trap early intermediates are lacking. Here we uncoverthe dynamics of the complete translation cycle in live yeast cells usingtranslation complex profile sequencing (TCP-Seq), a method developedfrom the ribosome profiling6 approach. We document scanningby observing SSU footprints along 5’UTRs. Scanning SSU have5’-extended footprints (up to 70 nt), indicative of additional interactionswith mRNA emerging from the exit channel, enforcing forwardmovement. We visualise changes in initiation complex conformationas SSU footprints coalesce into three major sizes at start codons (19,29 and 37 nt). These share the same 5’ start but differ at the 3’ end,reflecting successive changes at the entry channel from an open to aclosed state following start codon recognition. We also observe SSU‘lingering’ at stop codons after LSU departure. Our results underpinmechanistic models of translation initiation and termination, built ondecades of biochemical and structural investigation, with direct genomewide in vivo evidence. Our approach captures ribosomal complexesat all phases of translation and will aid in studying translation dynamicsin diverse cellular contexts. Dysregulation of translation is common indisease and, for example, SSU scanning is a target of anti cancer drugdevelopment. TCP-Seq will prove useful in discerning differences inmRNA-specific initiation in pathologies and their response to treatment.
Chen DavidovichEMBL Australia Group LeaderDepartment of Biochemistryand Molecular Biology, Schoolof Biomedical Sciences,Monash University, ARC Centreof Excellence in AdvancedMolecular Imaging, ClaytonCampus, Monash UniversityChen Davidovich is an EMBL-AustraliaGroup Leader in Monash University,studying the molecular events thatunderlie the recruitment and regulationof chromatin-modifying complexesby their co-factor proteins, RNAtranscripts and DNA. During his PhDstudy (Ada Yonath lab, WeizmannInstitute, 2004–2010) he usedX-ray crystallography to determinestructures of ribosomal complexes.In his postdoctoral study (Tom Cechlab, The University of Colorado atBoulder, 2010–2015), he focusedon studying the epigenetic modifierpolycomb repressive complex 2(PRC2) and its recruitment andregulation by long non-coding RNAs(lncRNAs) and RNA transcripts ingeneral; an arena he is still active in.Mechanism of RNA binding by thePolycomb repressive complex 2(PRC2)”Polycomb repressive complex-2 (PRC2) is a histone methyltransferaserequired for epigenetic silencing during development and in cancer.Among chromatin modifying factors that were shown to be recruitedand regulated by RNA, PRC2 is one of the most studied. MammalianPRC2 binds thousands of RNAs in vivo, including coding and longnon-coding RNAs (lncRNAs), and its histone methyl transferase activityis inhibited by RNA. We previously showed that PRC2 binds RNApromiscuously in vitro and in vivo. In contrast to nonspecific proteinRNA interactions, where various target RNAs are indistinguishable,promiscuous RNA binding by PRC2 allows it to discriminatetranscripts to a certain degree, though so far the mechanism wasobscured and binding motifs within target RNAs remained elusive. Wehave now identified low complexity RNA motifs that allow for variationsin affinity to PRC2. Although the PRC2-binding motif within RNAsis simple and low in complexity, multiple bases are required for highaffinity interactions. Such interactions with RNA involve multiple PRC2subunits. We will present new mechanistic information describingthe interactions between PRC2 and RNA, from both protein andRNA sides, and will describe a model for how these protein-RNAinteractions facilitate the maintenance of repressed chromatin.
Speaker BiosMichael ParkerEMBL Alumni, St. Vincent’sInstitute of Medical Institute andUniversity of MelbourneMichael Parker is Deputy Directorof St. Vincent’s Institute of MedicalResearch in Melbourne where heheads its Structural Biology Laboratoryand the ACRF Rational DrugDiscovery Centre. He is an NHMRCSenior Principal Research Fellowand a Professor at the University ofMelbourne. The work of the laboratoryis internationally recognised withthe determination of more than 140crystal structures including thoseof membrane-associating proteins,detoxifying enzymes and proteinkinases. He has published over300 papers and his work has beenrecognised with numerous awardsincluding the 1999 Gottschalk Medalof the Australian Academy of Science,a 2006 Federation Fellowship fromthe Australian Research Council, the2011 Lemberg Medal of the AustralianSociety for Biochemistry and MolecularBiology, the 2011 Ramaciotti Medalfor Excellence in Biomedical Researchand the 2012 Federation of Asian andOceanian Biochemists and MolecularBiologists Award for ResearchExcellence. He was elected a Fellowof the Australian Academy of Sciencein 2010 and a Fellow of the AustralianAcademy of Health and MedicalSciences in 2015. He is currentlyChair of the National Committee ofCrystallography under the auspices ofthe Australian Academy of Science.Cholesterol-dependent cytolysins:from water-soluble state tomembrane pore”The cholesterol-dependent cytolysins (CDCs) are one of the most widelydistributed toxins known, having been identified in 5 different genera ofGram-positive bacteria. The CDCs exhibit a number of unique featuresamongst pore-forming toxins including an absolute dependence on thepresence of cholesterol-rich membranes for their activity and the formationof oligomeric transmembrane pores greater than 150 Å in diameter. Thereare more than 20 members of the CDC family so far identified and thereexists a high degree of sequence homology (40–70%) suggesting theyall have similar activities and 3D structures. The first crystal structure ofa CDC was that of perfringolysin O1 and most of our understanding ofCDC function is based on studies of this toxin.2,3 We have subsequentlydetermined structures of other family members that have confirmed thatthe 3D fold first seen in PFO is shared by all family members.5–7 Functionalstudies have revealed that CDCs undergo a highly regulated stepwiseprocess in assembling as a large membrane pore consisting of more than30 monomers. Not only is the conversion from water-soluble monomer topore highly complex, it is essential that the pore does not form prematurelyotherwise the target cell won’t be successfully breached. The crystalstructures of the water-soluble states of these toxins, together withcryoelectron microscopy, small angle X-ray scattering data, fluorescencespectroscopy and molecular dynamics simulations have proved veryuseful for modelling their membrane pores.1. Rossjohn, J. et al., (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membraneform. Cell 89, 685–692.2. Shatursky, O. et al., (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novelparadigm for pore-forming toxins. Cell 99, 293–299.3. Gilbert, R.J. et al., (1999) Two structural transitions in membrane pore formation by pneumolysin, the pore-formingtoxin of Streptococcus pneumoniae. Cell 97, 647–6555. Polekhina, G. et al., (2005) Insights into the action of the superfamily of cholesterol-dependent cytolysins from studiesof intermedilysin. Proc. Natl. Acad. Sci. USA 102, 600–605.6. Feil, S.C. et al., (2012) Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysinreveals the molecular basis for its Lewis antigen specificity. Structure 20, 248–258.7. Feil, S.C. et al., (2014) Structural studies of Streptococcus pyogenes streptolysin O provides insights into the earlysteps of membrane penetration. J. Mol. Biol. 426, 785–792.
Max CryleEMBL Australia Group LeaderDepartment of Biochemistry andMolecular Biology, School ofBiomedical Sciences, MonashUniversity, ARCMax Cryle is an EMBL Australia Groupleader in the Victorian Node, based inthe Department of Biochemistry andMolecular Biology at Monash University.After obtaining his PhD in chemistry fromthe University of Queensland in 2006,he moved to the Max Planck Institutefor Medical Research in Heidelberg as aCross Disciplinary Fellow of the HumanFrontiers Science Program. He wassubsequently awarded funding from theGerman Research Foundation (DeutscheForschungsgemeinschaft) to establish hisown group to investigate glycopeptideantibiotic biosynthesis as part of theEmmy Noether program. His group worksat the boundary of chemistry and biology,where they apply a multidisciplinaryapproach including synthetic chemistry,biochemistry, structural biology andenzyme catalysis. In 2016 he joinedEMBL Australia to continue his researchinto understanding the biosynthesisof important natural antibiotics anddeveloping new antimicrobial agents. Hisgroup has made a number of importantbreakthroughs in understanding hownature synthesises the glycopeptideantibiotics, which are clinically relevantand synthetically complex molecules.For this work he was awarded the 2016Otto Schmeil prize by the HeidelbergAcademy of Arts and Sciences. Currently,his group is investigating the biosynthesisof several important antibiotics as well asinvestigating novel strategies and targetsfor antimicrobial development.Understanding Glycopeptide Antibioticbiosynthesis as a pathway to newantimicrobial agents”The glycopeptide antibiotics, which include the clinical compoundsteicoplanin and vancomycin, are natural products that we use in the lastline of medical defence against resistant Gram-positive bacterial infectionssuch as MRSA. The biosynthesis of the glycopeptide antibiotics centreson the actions and interplay of the peptide-producing non-ribosomalpeptide synthetase (NRPS) megaenzyme and the Oxy proteins, whichare members of the Cytochrome P450 superfamily of monooxygenases.These P450s are responsible for installing the multiple oxidative phenolicand aryl crosslinks between aromatic side chains of the linear precursorpeptide, finally yielding the glycopeptide antibiotic aglycones in theiractive 3D-conformation. As the production of all glycopeptide antibioticscurrently stems from in vivo biosynthesis, understanding the molecularprocesses behind their formation is crucial for future efforts to reengineerthe machinery and produce new glycopeptide antibiotics. Given that theoxidative crosslinking reactions performed by the Oxy proteins are not onlycrucial for antibiotic activity but also represent a significant challenge in thechemical synthesis of glycopeptide antibiotics, my group has concentratedon understanding this process. We have shown that the Oxy proteinsaccess their peptide substrates whilst they remain directly bound to theNRPS machinery: this occurs through recruitment by a conserved domainof previously unknown function, known as the X-domain. My team hasnow determined the structure of a complex of the X-domain with the firstOxy protein from teicoplanin biosynthesis, which reveals how this essentialrecruitment process is mediated on a molecular level during peptidematuration. In addition, we have characterised subsequent Oxy enzymesinvolved in the teicoplanin oxidative crosslinking cascade, which indicatesthat the enzymes involved in the teicoplanin oxidative cascade rely upondifferent active site architectures to bind their substrates in spite of theircommon mechanism and highly similar substrates.
Speaker BiosAndrew LonieDirector, EMBL AustraliaBioinformatics ResourceAndrew Lonie is Director ofthe Victorian Life SciencesComputation Initiative (VLSCI:http://vlsci.org.au), Director of theEMBL Australia BioinformaticsResource (EMBL-ABR: http://embl-abr.org.au), and an associateprofessor at the Faculty ofMedicine, Dentistry and HealthSciences at the University ofMelbourne, where he coordinatesthe MSc (Bioinformatics).Andrew directs a group ofbioinformaticians, computationalbiologists and HPC specialistswithin the VLSCI and EMBL-ABRto collaborate with and support lifesciences researchers in a variety ofresearch projects across Australia.Building the EMBL AustraliaBioinformatics Resource”The EMBL Australia Bioinformatics Resource is a distributednational research infrastructure providing bioinformatics supportto life science researchers in Australia. The Resource was setup as a collaboration with the European Bioinformatics Institute(EMBL-EBI) to maximise Australia’s bioinformatics capability. Thisclose partnership is made possible in the context of Australia’sassociate membership of EMBL. In this talk I will discuss progressin establishing the EMBL-ABR network including an overview ofactivities, strategic planning and funding.
Matthias W. HentzeEuropean Molecular BiologyLaboratory (EMBL), Heidelberg,GermanyMatthias Hentze is a native German. Heattended Münster University MedicalSchool, and studied at Oxford, Cambridge,Glasgow and Southampton. Followingon from his medical degree and a M.D. inBiochemistry (Münster), Matthias beganhis research career as a post-doctoralresearch fellow at the National Institutesof Health (Bethesda, Maryland, USA)before joining EMBL Heidelberg in 1989as a Group Leader. After obtaining theHabilitation from Heidelberg Universityin 1990, Matthias served as the Dean ofGraduate Studies from 1996 until 2005.In 2002 when he was Dean, Matthiasco-founded the Molecular MedicinePartnership Unit (MMPU) between EMBLand the Medical Faculty of HeidelbergUniversity which he still co-directs. Herethe Matthias research group conductstranslational research on common diseasesof iron metabolism and of altered mRNAmetabolism. In July of 2005, Matthias waspromoted from Dean to the position asEMBL Associate Director. In that sameyear, he became Professor for MolecularMedicine. As EMBL Director, Matthiasadvises and works closely with EMBL’sDirector General. Matthias oversees theareas of Resource Development andAlumni Relations, and is supported by theDirector’s Office. Matthias has many variedfunctions in his role, including supportingand representing the Director General atinternational scientific research, trainingand service organisations. Matthias alsogenerates additional opportunities for theLaboratory, by promoting aspects of EMBLvia public engagement and communicationstrategies as well as generating visibilityand positive awareness of the Laboratory.A new view on RNA-bindingproteins and RNA”We recently discovered that hundreds of cellular proteins, previouslywell known for other biological functions, also unexpectedly bind RNA(termed “enigmRBPs” for enigmatic RNA-Binding Proteins. Sincemany enigmRBPs are conserved from yeast to humans, their existenceraises pressing questions. One of the most stunning surprises wasthe discovery that almost all enzymes of the glycolytic pathway areconserved as enigmRBPs. Overall, more than 50 metabolic enzymeswere found to bind RNA. Could the combination of enzymatic andRNA-binding functions represent a general biological principle forcoordination between gene expression and metabolism? Applying anewly developed technique, RBDmap, to identify the RNA-bindingdomains of enigmRBPs, we uncovered new RNA-binding architecturesyielding functional insights. Integrating all information, we discuss apossible new function for genomes in addition to their classical role indriving protein biosynthesis via mRNAs, rRNAs, and tRNAs and theirassociated modifying and regulatory RNAs.
Speaker BiosMirana RamialisonResearch Group LeaderScientific Liaison Officer,South AmericaMirana is head of the SystemsDevelopmental Biology Laboratoryat the Australian RegenerativeMedicine Instit
Medicine Institute, Monash University Edwina McGlinn is an EMBL- Australia Partner Network Lab Group Leader, based at the Australian Regenerative Medicine Institute, Monash University. . interaction networks in cancer. His Group is currently supported by: EMBL Australia, The Europea
Motivation: Personalised studies of variation, cancer mutation, epigenetics, regulation, expression require references for comparison and interpretation As part of GA4GH, EMBL-EBI is working on Resou
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