A hot species for cool structures: Complex proteins in 3-D thanks to simple heat-loving fungus

Jul 21, 2011

A fungus that lives at extremely high temperatures could help understand structures within our own cells. Scientists at the European Molecular Biology Laboratory (EMBL) and Heidelberg University, both in Heidelberg, Germany, were the first to sequence and analyse the genome of a heat-loving fungus, and used that information to determine the long sought 3-dimensional structure of the inner ring of the nuclear pore. The study was published today in Cell.

The Chaetomium thermophilum lives in soil, dung and compost heaps, at temperatures up to 60 C. This means its proteins – including some which are very similar to our own – have to be very stable, and the Heidelberg scientists saw this stability as an advantage.

"There are a number of structures that we couldn't study before, because they are too unstable in organisms that live at more moderate temperatures," explains Peer Bork, who led the analysis at EMBL. "Now with this heat-loving fungus, we can."

The scientists compared the fungus' genome and proteome to those of other eukaryotes – organisms whose cells have a nucleus – and identified the proteins that make up the innermost ring of the , a channel that controls what enters and exits a cell's nucleus. Having identified the relevant building blocks, the scientists determined the complex 3D structure of that inner ring for the first time.

"This work shows the power of interdisciplinary collaborations," says Ed Hurt, who led the structural and biochemical analyses at Heidelberg University: "the nuclear pore is an intricate biological puzzle, but by combining bioinformatics with biochemistry and structural biology, we were able to solve this piece of it for the first time."

The scientists have made C. thermophilum's genome and proteome publicly available, and are confident that these will prove valuable for studying other eukaryotic structures and their interactions, as well as general adaptations to life in hot places. Such knowledge could potentially lead to new biotechnology applications.

Explore further: New knowledge about host-virus coevolution unmasked from the genomic record

More information: Published online in Cell on 22 July 2011.

add to favorites email to friend print save as pdf

Related Stories

Membrane-coat proteins: Bacteria have them too

Jan 20, 2010

Although they are present almost everywhere, on land and sea, a group of related bacteria in the superphylum Planctomycetes-Verrucomicrobia-Chlamydiae, or PVC, have remained in relative obscurity ever since ...

Recommended for you

Devising a way to count proteins as they group

2 hours ago

A new study from Indiana University-Purdue University Indianapolis and University of California Berkeley researchers reports on an innovative theoretical methodology to solve "the counting problem," which is key to understanding ...

Mysteries of 'molecular machines' revealed

3 hours ago

"Inside each cell in our bodies and inside every bacterium and virus are tiny but complex protein molecules that synthesize chemicals, replicate genetic material, turn each other on and off, and transport ...

Bacteria are wishing you a Merry Xmas

9 hours ago

A bacterium has been used to wish people a Merry Xmas. Grown by Dr Munehiro Asally, an Assistant Professor at the University of Warwick, the letters used to spell MERRY XMAS are made of Bacillus subtilis, ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.