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Oxygen key to ‘cut and paste’ of genes

3 July 2009 

An oxygen-sensitive enzyme has been found to play a key role in how genes create the many different proteins that make up our bodies.

The finding shows that the enzyme, termed Jmjd6, directly intervenes in the process in which the DNA of our genes is ‘cut and pasted’ into instructions for the creation of specific proteins. 

The discovery, reported in this week’s Science by a team led by scientists from Oxford University and Ludwig-Maximilians-University, Munich, opens up a new area of molecular research into conditions such as heart disease and cancer. 

‘Previous work from Oxford has shown that some of these enzymes, called oxgenases, affect which genes are expressed in response to low levels of oxygen. What we have now found is that they also regulate the specific form this expression takes – to give the different proteins that make up everything from heart cells to tumours.’ said Professor Chris Schofield of Oxford University’s Department of Chemistry, one of the authors of the paper.

Genes, stored in the form of DNA, are converted into proteins by a ‘middleman molecule’ called Messenger Ribonucleic Acid - or ‘mRNA’. 

Individual genes can often give rise to many different proteins because of a process known as mRNA splicing which enables the cutting and pasting of the mRNA that is produced from DNA. The proteins that the new oxygenase, termed Jmjd6, acts on are involved in regulating the 'cutting and pasting' process. 

Angelika Böttger, who led the Munich group, said: ‘The discovery of a role for an oxygenase in mRNA splicing reveals that it is very likely that oxygen levels are involved in regulating almost all steps in the process of gene expression. The challenge now is to determine how the pattern of genes changes in different environments when oxygen is in short supply, enabling us to tackle important questions such as ‘why do tumour cells respond differently to low oxygen levels than normal cells?’’

For further information contact Professor Chris Schofield on +44 (0)1865 275625 [mobile: +44 (0)7811 280977] or email

christopher.schofield@chem.ox.ac.uk Alternatively, contact the University of Oxford Press Office on +44 (0)1865 283877 or email press.office@admin.ox.ac.uk 

Notes to editors

  • A report of the research, entitled ‘Jmjd6 catalyses lysl-hydroxylation of U2AF65, a protein associated with RNA splicing,’ is published in this week’s Science under embargo until 19:00 BST, 2 July 2009.
  • The research was conducted by an international team including scientists from Oxford University (UK), Ludwig-Maximilians-University, Munich (Germany), Max-Planck-Institute of Biochemistry (Germany), The Scripps Research Institute (USA), Helmhotz Centre for Infection Research (Germany), and the University of Edinburgh (UK).
  • Because oxygen is an essential source of energy for all animals, including humans, we have developed mechanisms for sensing and responding to changes in oxygen levels. For example if we are at high altitude our bodies respond by making more red blood cells. Oxygenases add oxygen atoms directly from oxygen in the atmosphere to proteins. The addition of oxygen atoms regulates the function of proteins in a manner that changes with availability of atmospheric oxygen - with less oxygen the oxygenases work less well - with more they work better.