Pioneering University of Leicester research to be showcased in Parliament
Issued by University of Leicester Press Office on 15 February 2011
A celebration in Parliament of the work of emerging scientific, engineering and technological leaders is to showcase the work of a University of Leicester biochemist on 14th March.
The work of Dr Cyril Dominguez, a Lecturer and MRC Research Fellow in the Leicester Department of Biochemistry, was selected for this honour as part of the SET for BRITAIN Awards.
Selection for participation is made solely on the basis of the very best research work and results by researchers at an early stage in their career.
The aim is to encourage, support and promote Britain's early-stage and early-career research scientists, engineers and technologists who are the "engine-room" of continued progress in, and development of, UK research and R&D, and ultimately of UK plc.
The occasion will present work by Dr Dominguez that sheds new light on how RNA binding proteins can affect cellular functions in a process known as ‘alternative splicing’ which is associated with many genetic diseases and with cancer.
Dr Dominguez commented:“For many years, it was thought that messenger RNAs were passive molecules that transferred the information from the genomic DNA to the proteins.
However, the human genome sequencing project identified only around 20,000 genes in human, which was unexpectedly low compared with the > 100,000 different proteins that can be produced.
We now know that this discrepancy is resolved by alternative splicing, a mechanism that is very important in cells to generate such a protein diversity from a limited number of genes. It has been recently shown that more than 90% of the human genes are alternatively spliced.”
Professor of Structural Biology and Head of the Department of Biochemistry at Leicester, Professor John Schwabe commented:"Dr Dominguez is clearly a rising star and we are delighted to have attracted him to the Department."
Notes to Editors: The title of Dr Dominguez’s presentation and a more detailed explanation follows. Further details are available from Dr Cyril Dominguez, Department of Biochemistry, University of Leicester,
Tel: 0116 229 7073, Email: email@example.com
STRUCTURAL BASIS OF G-TRACT RECOGNITION BY hnRNP F qRRMs: SPLICING REGULATION BY RNA STRUCTURE DESTABILIZATION
In humans, the synthesis of proteins from genes is a complex and highly regulated mechanism that involves many modifications of the RNA, such as alternative splicing, and allows for the generation of multiple protein isoforms from a single gene.
The regulation of alternative splicing is a major cellular event involving the binding of proteins to specific sequences of the RNA. The hnRNP F/H family consists of four RNA binding proteins that regulate many aspects of RNA metabolism by specifically recognizing Guanine-tracts in RNA.
Dr Dominguez’s presentation will show the structure of one member (hnRNP F) in complex with G-tract RNA that reveals the molecular basis of G-tract recognition.
The mode of binding observed is remarkably different from any other known RNA binding domain, defining a new class of RNA binding domain that could be detected in several additional human proteins.
The study suggests a novel mechanism of action where hnRNP F regulates alternative splicing by remodelling RNA structure.