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LABORATORY OF EVOLUTION AND STRUCTURAL BIOLOGY

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RESEARCH

Our Philosophy

In plain English: The driving principle of the laboratory is that shape defines function. This laboratory uses structural biology to “see” the protein components of biological machines. Through understanding how the parts fit together, and how the components move relative to each other, we being to understand what these biological machines do, and how and why they work. Specifically, the “designs” of protein machines have been perfected (selected for) over several billion years of evolution. Through comparing the genomes from organisms that have diverged at different time points in evolution, we chart the paths of how protein machines have become more sophisticated in carrying out their functions. 

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THE GODS OF THE ACTIN CYTOSKELETON

Asgard archaea are named after the gods of Norse mythology, including Heimdall, Loki, Odin, Thor, Hel and Gerd. Metagenomics sequencing has revealed that Asgard archaea contain potential homologs to eukaryotic genes. Several of these gene products are involved in forming the cytoskeleton and modifying membranes, hallmarks of eukaryotic cells. Thus, the hypothesis that the source eukaryotic cell arose from the Archaea domain now has potential model organisms to study that may have the pre-eukaryotic properties. However, only one Asgard archaea has been successfully imaged and cultivated, bringing in to question whether these archaea generally exhibit eukaryotic characteristics. Recently, we published evidence that the Asgard versions of the actin and its regulators, profilins and gelsolins, are functional at the protein level. In eukaryotes, force from directed actin polymerization drives membrane remodelling through filament nucleation and elongation machineries such as formins, which recruit the profilin/actin complex to initiate polymerization. Many of these interactions are regulated by the phospholipid PIP2. We demonstrated that LokiProfilin is a true profilin being functional in regulating mammalian actin in vitro. We determined the LokiProfilin/mammalian actin crystal structure, which verified the conserved actin interaction (above). Asgard profilins appear to be primitive actin regulators since they do not interact with formin polyproline sequences but do interact with phospholipids, features of eukaryotic profilins. Through structural and biochemical studies we have discovered that some thorarchaeota gelsolins (2DGel) are able sever actin filaments in a calcium-dependent manner, whilst single domain ProGels are more similar to cofilin, in their binding to actin.  Hence, we have generated the first experimental data at the protein level that suggests that eukaryotes may have evolved from the Archaea domain. Here, we will build on these initial findings to study other eukaryotic-like proteins encoded from the Asgard genomes.

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WHERE IS LOKI?

by Yuki Kawada

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ROBERT (BOB) ROBINSON

Bob obtained a BSc (1987)in Chemistry from King's College, London University, an MSc (1990) in Biochemistry from University of British Columbia, and a DPhil (1996) in Structural Biology from Oxford University.  During his postdoctoral studies at the Salk Institute for Biological Studies (1996-2001), Bob solved the X-ray structure of Arp2/3, an actin-nucleating complex consisting of seven proteins. In 2001, Bob was appointed as a Senior Lecturer at Uppsala University. There, the research group continued to elucidate structures of key actin-regulating proteins. Bob became an EMBO Young Investigator in 2003. Bob joined IMCB, Singapore as a Principal Investigatorin 2005 and became a Research Director in 2011. Bob joined RIIS in 2018 as a professor. From 2023, Bob became a full time Professor at VISTEC, Thailand and a Visiting Professor in Okayama University.

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March 2022

Spring - out with the old

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OPPORTUNITIES IN THE ROBINSON LABORATORY

We are looking for bright, enthusiastic people with a sense of fun and a curiosity in science.

INTERNATIONAL PHD STUDENTS

Application deadlines in January and June each year.

Applicants should hold a MSc degree at the time of course commencement. Interested applicants should contact Bob at br.okayama.u@gmail.com.

JAPANESE PHD STUDENTS

Application deadlines in January and August each year.

Come and join our international laboratory. Interested applicants should contact Bob at br.okayama.u@gmail.com.

POSTDOCS

Open

We have no funding to hire postdocs at present. Self-funded postdocs or applicants willing to apply for fellowships should contact Bob at br.okayama.u@gmail.com.

MASTERS STUDENTS

April or October

2 year course.

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VISITORS TO THE LAB

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August 2019
From Diamond Light Source
Oxfordshire
UK

Correlative X-ray tomography and fluorescence

imaging workshop

Visitors to the Lab
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GET IN TOUCH


Research Institute of Interdisciplinary Science
Okayama University
3-1-1 Tsushimanaka
Kita-Ku
Okayama-shi
700-8530

+81 86-251-7820

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