My biochemical journey from a Cambridge undergraduate to the discovery of phosphotyrosine

The most notable moment in my career as a biochemist was the discovery of phosphotyrosine, a somewhat serendipitous finding that turned out to have some very important consequences, notably, in human cancer. My career as a biochemist which has spanned nearly 60 years, began when I was 16. At the time, I was in the sixth form at Felsted School, a boarding school in Essex England, and my biology master, David Sturdy, elected to teach me some extracurricular biochemistry, giving me one-on-one tutorials on glycolysis and the TCA cycle. These early biochemistry lessons turned out to be invaluable because I was able to regurgitate them to answer a question in the University of Cambridge scholarship exam in the autumn of 1960. As a result, I was lucky enough to be awarded an Exhibition at Gonville and Caius College, the college where my father had studied for a medical degree during World War II. When I arrived in Cambridge in October 1962 to read natural sciences (see Figure 1), it was a natural choice to take biochemistry as one of my three required first-year courses. The Part I biochemistry course was taught by a series of excellent lecturers, including Philip Randle (a prominent diabetes researcher who described the Randle Cycle), Brian Chappell (who discovered mitochondrial transporters) and Asher Korner (a pioneer of cell free systems to study protein synthesis). It quickly became clear that biochemistry was an exciting subject, and Brian Chappell, my biochemistry supervisor at Caius, made supervisions a lot of fun. I also took Part I courses in invertebrate zoology and, importantly, organic chemistry, which gave me insights into how the metabolites we were learning about in biochemistry worked as chemicals.

HeLa at 70: on honouring the legacy of Henrietta Lacks

The 4th of october 2021 signified 70 years since the untimely death of Henrietta Lacks, a daughter, wife and mother. On the same day, the University of Bristol unveiled a statue of Henrietta that sits in the heart of its campus in Royal Fort Gardens, by local artist Helen Wilson-Roe. The unveiling came amidst a year of celebratory events for the legacy of a woman whose contribution to science is, in many ways, unrivalled. To many cell biologists, Henrietta Lacks is a household name; however, to the general public her name remains largely unknown. So, who is Henrietta Lacks? And why are the Lacks family and their family-led HELA100 initiative working in collaboration with the University of Bristol to honour her legacy?

A pandemic in the age of next-generation sequencing

Since December 2019, the world has found itself rocked by the emergence of a highly contagious novel coronavirus disease, COVID-19, caused by the virus SARS-CoV-2. The global scientific community has rapidly come together to understand the virus and identify potential treatments and vaccine strategies to minimise the impact on public health. Key to this has been the use of cutting-edge technological advances in DNA and RNA sequencing, allowing identification of changes in the viral genome sequence as the infection spreads. This approach has allowed a widespread ‘genomic epidemiology’ approach to infection control, whereby viral transmission (e.g. in healthcare settings) can be detected not only by epidemiological assessment, but also by identifying similarities between viral sub-types among individuals. The UK has been at the forefront of this response, with researchers collaborating with public health agencies and NHS Trusts across the UK to form the COVID-19 Genomics UK (COG-UK) Consortium. Genomic surveillance at this scale has provided critical insight into the virulence and transmission of the virus, enabling near real-time monitoring of variants of concern and informing infection control measures on local, national and global scales. In the future, next-generation sequencing technologies, such as nanopore sequencing, are likely to become ubiquitous in diagnostic and healthcare settings, marking the transition to a new era of molecular medicine.

CRISPR systems: what’s new, where next?

The genetic signature of natural CRISPR-Cas systems were first noted in a 1989 publication and were characterized in detail from 2002 to 2007, culminating in the first report of a prokaryotic adaptive immune system. Since then, CRISPR-Cas enzymes have been adapted into molecular biology tools that have transformed genetic engineering across domains of life. In this feature article, we describe origins, uses and futures of CRISPR-Cas enzymes in genetic engineering: we highlight advances made in the past 10 years. Central to these advances is appreciation of interplay between CRISPR engineering and DNA repair. We highlight how this relationship has been manipulated to create further advances in the development of gene editing.

Glycans for the greater good

Carbohydrates are ubiquitous in nature and present across all kingdoms of life – bacteria, fungi, viruses, yeast, plants, animals and humans. They are essential to many biological processes. However, due to their complexity and heterogeneous nature they are often neglected, sometimes referred to as the ‘dark matter’ of biology. Nevertheless, due to their extensive biological impact on health and disease, glycans and the field of glycobiology have become increasingly popular in recent years, giving rise to glycan-based drug development and therapeutics. Forecasting of communicable diseases predicts that we will see an increase in pandemics of humans and livestock due to global loss of biodiversity from changes to land use, intensification of agriculture, climate change and disruption of ecosystems. As such, the development of point-of-care devices to detect pathogens is vital to prevent the transmission of infectious disease, as we have seen with the COVID-19 pandemic. So, can glycans be exploited to detect COVID-19 and other infectious diseases? And is this technology sensitive and accurate? Here, I discuss the structure and function of glycans, the current glycan-based therapeutics and how glycan binding can be exploited for detection of infectious disease, like COVID-19.

The algae revolution 2.0: the potential of algae for the production of food, feed, fuel and bioproducts – why we need it now

Algae made our world possible, and it can help us make the future more sustainable; but we need to change the way we live and adopt new more efficient production systems, and we need to do that now. When the world was new, the atmosphere was mainly carbon dioxide, and no animal life was possible. Along came algae with the process of photosynthesis, and things began to change. Ancient cyanobacteria algae turned carbon dioxide into enormous sums of lipids, proteins and carbohydrates, while they secreted oxygen into the atmosphere. Over a billion years, as oxygen filled the air and algae filled the seas, animal life became possible. Eventually all that algae biomass became petroleum and natural gas, which for eons sat undisturbed in vast underground reservoirs, holding enormous sums of untapped energy. Less than 200 years ago humans learned to tap these energy reserves to create the world we know today, but in so doing, we have released millions of years of stored CO2 back into the atmosphere. Algae can again help make the world a better place, but this will require new thinking and new ways of producing our food, feed and fuels. We need an algae revolution 2.0.

Opportunities for early-career researchers to engage with science policy through the Biochemical Society

Science policy can be broadly defined as a two-way dialogue between science-related sectors and government. It involves the exchange of scientific findings and opinions with policy makers to inform the decision-making process, as well as the scrutinization of legislation around science-related topics to ensure it is based on sound evidence. Science policy covers a variety of issues, including research, education, funding, ethics, public health and equality, diversity and inclusion (EDI).