Australia - Scientists Solve Molecular Structure Of Protein Complex That Turns Cancer On And Off

Australian researchers, using a combination of microscopy and X-ray crystallography techniques, have solved a new molecular structure formed by two human proteins involved in turning genes on and off in cancer.

This groundbreaking study, published in the Proceedings of the National Academy of Sciences of the USA, revealed the atomic structure of two proteins, NONO and PSPC1, bound together and forming a complex called a paraspeckle.

Paraspeckles, discovered by co-author Dr. Archa Fox in 2001, are irregularly shaped structures found scattered in the interchromatin space of the cell nucleus, and are thought to be involved in directing proteins to appropriate areas for their biological function.

The researchers, from the University of Western Australia (UWA) and Western Australian Institute for Medical Research (WAIMR), improvised their experimental strategy by complementing crystallography with microscopy, which not only revealed the combined structure of the proteins but also the location in the cell where these proteins act.

The team also made use of the Australian Synchrotron’s Macromolecular Crystallography and Small-angle X-ray Scattering facilities to solve the structures of the interlocking proteins.

“Proteins in our cells are like very tiny machines,” said lead-author Professor Bond. “In order to understand how they work and develop drugs against them, we have to magnify them. By combining microscopy and a sophisticated technique called crystallography, we have been able to observe the detailed atomic structure of NONO and PSPC1, and their location in the cell.”

The research is still at the infancy stage, said co-author Dr. Archa Fox, who added that it is the first step towards developing drugs that could change the way these proteins work.

Yuka Suzuki

AsianScientist

The article can be found at: Passon DM et al. (2012) Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation.

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