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| Heidelberg,
Sunday, 19 June 2005 |
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| A link between our body's energy levels and a protein that wraps our DNA? |
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| PhD student Georg Kustatscher and Dr. Andreas Ladurner. |
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Press
Release 21 June 2005 [PDF]
Scientists discover a connection between a histone and a metabolite
Living organisms need to sense the amount of energy
that is available to them and regulate the activity
of their genes accordingly. Scientists have made
the unexpected finding that a histone protein, which
wraps DNA into tight bundles and regulates gene
activity, can bind a small molecule produced in
our cells. This novel finding in itself was a breakthrough
for researchers at the European Molecular Biology
Laboratory [EMBL], but what made it more interesting
was which specific molecule it binds – one from
a pathway known to be linked to obesity and aging.
The EMBL researchers studied a pathway involving
an enzyme [Sir2], whose activity is regulated by
the availability of nutrients, and an energy molecule
[NAD]. This pathway, and the enzyme Sir2 in particular,
has been heavily investigated because nutrients
are known to regulate Sir2's activity on genes.
"Each enzyme's job is to turn starting materials
into final products. These usually have important
functions, but while several scientists have studied
the enzyme Sir2, no one has identified a role for
one of the final products of the reaction in humans,"
says EMBL Group Leader Andreas Ladurner.
When Sir2
binds to NAD, it breaks down the energy molecule
into smaller components. What the EMBL researchers
found was that one of these components plugs neatly
into a special pocket of the histone that the researchers
were studying.
This discovery is the first evidence
of a small compound binding directly to a histone.
As the activity of Sir2 is regulated by the amount
of food and nutrients, this finding suggests the
existence of a direct link between one of the products
of the Sir2 pathway and gene regulation.
"It is very exciting that a histone should
be able to recognize one of the compounds that Sir2
produces. We are now looking at how such a small
molecule may be able to tweak our genes and therefore
our body's response to changes in the availability
of food and energy," Ladurner says. PhD student
Georg Kustatscher and Dr. Andreas Ladurner
Source Article
Splicing regulates NAD metabolite binding to
histone macroH2A
G. Kustatscher, M. Hothorn, C. Pugieux, K. Scheffzek and A. Ladurner
Nature Structural and Molecular Biology,
19 June 2005
Press Contact
Trista Dawson
EMBL Press Officer, European Molecular Biology Laboratory,
Meyerhofstrasse 1, 69117 Heidelberg, Germany
Tel: +49 [0] 6221 3878452
E-mail: trista.dawson@embl.de |
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