Ada Lovelace day20 November 2015On the 18th November, the Equality & Diversity and Widening Participation offices welcomed over 100 schoolchildren to take part in a Science Showcase as part of the University's celebrations of Ada Lovelace's 200th birthday.
Bristol Biochemistry undergraduate student wins poster prize7 October 2015Congratulations to Rebecca Dixon-Steele, one of our final year undergraduate students, on winning the best poster prize at the Drug Discovery 2015 conference in Telford, organised by ELRIG. Rebecca gave a 10 minute presentation in a poster taster session in the ‘Innovation in Assay Development and Screening’ track, winning her the best poster prize.
DNA shredding by a bacterial enzyme22 September 2015The integrity of the genetic information stored in DNA relies on maintenance of its double-stranded structure. Nonetheless, cells sometimes need to break DNA by cutting each of the polynucleotide strands. These DNA cleavage events are catalysed by enzymes called nucleases; nature’s molecular scissors. Many nucleases are complexes of two proteins, one subunit to cut each DNA strand (i.e., each subunit is a blade of the molecular scissors). A dimer structure ensures that the cuts are close together, leading to a simple DNA break. A collaboration between research teams in Bristol and Pune, India, has now revealed an alternative mechanism, where a pair of nuclease subunits are held distantly apart and the DNA cleavage is more ragged.
Congratulations to our Students!22 July 2015The School is delighted to congratulate its undergraduate students from all years on an excellent set of examination results, perpetuating the strength and reputation of the Bristol Biochemistry degree programmes.
Cancer surgery or biopsy collection could influence disease progression2 July 2015Scientists at Bristol Biochemistry studying the body’s inflammatory response to wounds following cancer surgery or biopsy have found that these procedures may cause growth signals to be delivered to any remaining cancer or pre-cancerous cells which may negatively influence disease progression.
Bristol Biochemistry Academic Scoops Two Teaching Awards26 June 2015The winners of the 2015 Bristol Teaching Awards have been announced on Monday 15th June. The Bristol Teaching Awards are a joint venture between the University of Bristol and Bristol SU (the Students’ Union). The Awards are to recognise the most outstanding members of staff who have delivered exceptional contributions to teaching and supporting students.
Human trials of manufactured blood within two years25 June 2015The first human trials of lab-produced blood to help create better-matched blood for patients with complex blood conditions has been announced by NHS Blood and Transplant. Research led by scientists at the University of Bristol and NHS Blood and Transplant, used stem cells from adult and umbilical cord blood to create a small volume of manufactured red blood cells.
ESCRT-III controls nuclear envelope reformation4 June 2015Mitosis is the process by which eukaryotic cells divide up their chromosomes and form two genetically identical daughter cells. It involves a series of highly co-ordinated steps mediated by a plethora of proteins. During the final stages of mitosis (telophase) the nuclear envelope reassembles around the segregated chromosomes in a two-step process first involving the coating of chromatin by membranes from the endoplasmic reticulum followed by annular fusion of these membranes together to create a sealed barrier. Staff and Facilities of the School of Biochemistry collaborated with King's College London to investigate this, culminating in a publication in Nature.
Molecular basis of rapamycin insensitivity of Target Of Rapamycin Complex 2 revealed1 June 2015In eukaryotes, cell growth and division is stimulated by the availability of nutrients, presence of growth factors and of other cells. One of the key factors controlling cell growths is Target Of Rapamycin (TOR), a conserved, atypical protein kinase which is an important cancer therapeutic target and which is inhibited by the immunosuppressive, anti-proliferative drug rapamycin in complex with the FKBP12 protein. Decreased TOR activity has been found to increase life span in S. cerevisiae, C. elegans and mice. TOR kinase is part of two very large multi-protein complexes: rapamycin-sensitive TOR complex 1 (TORC1) and rapamycin-insensitive TOR complex 2 (TORC2). Why TORC2 is insensitive to rapamycin has been a longstanding mystery in the TOR field. In a paper published by Molecular Cell, this essential question has now been answered.
Pint of Science12 May 2015Several members of the School of Biochemistry's staff and students are discussing their science with the public in pubs across Bristol as part of the national Pint of Science festival taking place 18th-20th May
Wishing farewell and good luck to Dr Mark Bass20 March 2015Dr Mark Bass joined the School of Biochemistry in November 2009 as Wellcome Trust funded Research Fellow, and is now moving on to a permanent Lectureship in the University of Sheffield.
Bristol awarded share of £40 million investment for UK synthetic biology30 January 2015The University of Bristol has been awarded a share of £2.2 million as part of a new £40 million investment for UK synthetic biology. Business Secretary Vince Cable announced the multi-million investment at the Manchester Institute for Biotechnology, where researchers are using the technology to investigate how to use bacteria in place of fossil fuels to produce the chemicals we need to manufacture a wide variety of everyday products from credit cards, to nappies, to Tupperware tubs
Cellular assembly mechanisms of essential transcription factor complex revealed23 January 2015Our cells contain a plethora of proteins that catalyse biological activity. Typically these proteins do not act alone. Rather they form large multicomponent assemblies that, in humans, often contain 10 or more subunits. For instance the machinery that reads out our genes is composed of more than 100 proteins. The cell exploits this astounding complexity to meticulously fine-tune gene expression in the cell nucleus, which contains our genome.
Vital cornerstones of this process are the general transcription factors (GTFs) which together recruit RNA polymerase II, the enzyme that transcribes genes into messenger RNA. The largest human general transcription factor is TFIID, a megadalton-sized multiprotein complex containing 22 subunits. TFIID was discovered more than two decades ago, and much effort has been expended to elucidate its structure and function. How our cells manage to assemble TFIID from its individual components, however, remained entirely enigmatic.