Enzyme Discovery Increases Scope for Breaking Down Plastics


The enzymes (PETase and MHETase) break the PET polymer into the chemical building blocks ethylene glycol (EG) and TPA.


“While EG is a chemical with many uses – it’s part of the antifreeze you put into your car, for example – TPA does not have many uses outside of PET, nor is it something that most bacteria can even digest,” said lead author Professor DuBois from Montana State University. “However, the Portsmouth team revealed that an enzyme from PET- consuming bacteria recognises TPA like a hand in a glove. Our group at MSU then demonstrated that this enzyme, called TPADO, breaks down TPA and pretty much only TPA, with amazing effi ciency.”


Professor John McGeehan, Director of the University’s Centre for Enzyme Innovation. (Credit: University of Portsmouth)


As part of the UK/US Bottle Consortium project to tackle plastic recycling and upcycling, scientists have used Diamond’s macromolecular crystallography (MX) beamline I03 to characterise an enzyme capable of breaking down terephthalate (TPA), one of the chemical building blocks of polyethylene terephthalate (PET) plastic, widely used in-single use items such as drinks bottles.


The research [1], was co-led by Professor Jen DuBois, Montana State Universit, and Professor John McGeehan from the University of Portsmouth, who in 2018 led


the international team that


engineered a natural enzyme that could break down PET plastic drinks bottles, clothing and carpets.


Lead author and experienced Diamond user Professor McGeehan, who is the Director of the University of Portsmouth’s Centre for Enzyme Innovation, said: “The last few years have seen incredible advances in the engineering of enzymes to break down PET plastic into its building blocks. This work goes a stage further and looks at the fi rst enzyme in a cascade that can deconstruct those building blocks into simpler molecules. These can then be utilised by bacteria to generate sustainable chemicals and materials, essential making valuable products out of plastic waste.


“Using powerful X-rays at Diamond Light Source, we were able to generate a detailed 3D structure of the TPADO enzyme, revealing how it performs this crucial reaction. This provides researchers with a blueprint for engineering faster and more effi cient versions of this complex enzyme.”


With more than 400 million tons of plastic waste produced each year, the overwhelming majority of which ends up in landfi lls, it is hoped this work will open the door to improve bacterial enzymes, such as TPADO. This will help tackle the challenge of plastic pollution and develop biological systems that can convert waste plastic into valuable products.


The TPADO enzyme (Credit: Rita Clare, Montana State University)


1. Kincannon W.M. et al. Biochemical and structural characterization of anaromatic ring–hydroxylating dioxygenase for terephthalicacid catabolism. PNAS (2002). DOI: 10.1073/pnas.2121426


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RMS: Abercrombie Meeting Oxford September 2022


Michael Abercrombie was a pioneer in the fi eld of investigating cell behaviour using timelapse microscopy and this series of meetings, held only every fi ve years offer an excellent opportunity to review the major advances in our understanding of cell motility and look to the new emerging concepts in the fi eld.


The RMS is now inviting both oral and poster presentations for the next Abercrombie meeting to be held this year at the University of Oxford, 12-14 September.


Scientifi c Organisers: Dr Brian Stramer, King’s College London


Brian is a group leader at the Randall Division of Cell and Molecular Biophysics at King’s College London. He received his PhD in 2003 in Cell, Molecular and Developmental biology from Tufts University in Boston, Massachusetts, USA, and subsequently received a US/UK Royal Society Postdoctoral Fellowship to work in the laboratory of Paul Martin at the University of Bristol.


In 2008, he obtained an independent group leader position at King’s College London where he started his work on the basic mechanisms of cell migration and its roles during embryogenesis.


Professor Ewa Paluch, University of Cambridge, UK Dr Gaudenz Danuser, UT Southwestern Medical Center, Dallas


Gaudenz Danuser is an engineer (geodetic and electrical engineering/ computer science) who started to transition into cell biology as a postdoctoral fellow in the Program for Architectural Dynamics of Living Cells at the MBL in Woods Hole. He has primarily focused his research on the question of how chemical and mechanical signals integrate in the regulation of cytoskeleton dynamics and membrane traffi cking. A teacher in areas of computational cell biology, machine learning, cellular biophysics and the theory of measurement applied to cell biology both at the institutional and international level, he is currently chairman of the Lyda Hill Department of Bioinformatics at UT Southwestern Medical Center in Dallas, where he is also the Director of the Cecil H. and Ida Green Center of Systems Biology.


Ewa is a physicist who transitioned towards cellular biophysics during her Masters and PhD at the Curie Institute in Paris. She started her research group in 2006 at the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden (joint appointment with the IIMCB, Warsaw), with a focus on investigating the mechanics of the cellular actin cortex and its contribution to the control of cell shape. Early projects in the lab focused on investigating the regulation and function of blebs in cell migration. In 2013, Ewa was appointed Professor of Cell Biophysics at the MRC LMCB, University College London, and in 2018, she was elected Chair of Anatomy at the University of Cambridge, UK. The Paluch lab is currently located at the Department of Physiology, Development and Neuroscience at the University of Cambridge.


Abstracts should be emailed to katiereynolds@rms.org.uk. Please include in your email whether you would prefer to be considered for an Oral or Poster presentation.


Abstract submission deadline is 28th April. More information online: ilmt.co/PL/2zdV


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RMS Early Career Award Winner Revealed


Commending her studies in membrane traffi cking pathways the RMS is delighted to announce Katherine Paine of the University of York as the winner of its 2022 Early Career Award. Katherine, who began her PhD in 2018 at Chris MacDonald’s laboratory, was chosen in recognition of the novel approaches in imaging and cytometry she has brought to her studies on the regulation of cell surface membrane proteins.


She will receive a £100 cash prize and an invitation to deliver a keynote presentation at Microscopy: Advances, Innovation, Impact 2022 – an event which includes the RMS Annual General Meetings.


RMS Early Career Committee Chair, Liam Rooney said: “Not only have Katherine’s approaches allowed her to discover novel mechanisms related to surface protein traffi cking in yeast, but these methods can now be used by others in the fi eld in the future. It is a privilege to commend her achievements with this award.”


Katherine Paine


Cell surface membrane proteins perform diverse and critical functions and are spatially and temporally regulated by membrane


traffi cking pathways, a process evolutionary conserved from yeast to humans. MacDonald lab uses yeast as a model organism to study these pathways.


Initially using standard confocal microscopy, it became clear that this alone presented limitations in visualisation of some of the processes of interest. This led to Katherine helping with optimisation of a suite of imaging and cytometry approaches to study surface proteins, including Airyscan2, structured illumination (SIM) and photoactivated localisation microscopy (PALM); all of which can be coupled to bespoke microfl uidic exchange systems.


Katherine is also in the process of optimising a high throughput method to measure Förster resonance energy transfer (FRET) in yeast using robotics and fl ow cytometry.


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