Polarized microscopy technique shows new details of how proteins are arranged

April 19, 2011

Using polarized light microscopy, researchers show that Y-shaped subcomplexes of the nuclear pore complex are arranged head to tail (left) and that an alternative “fence-post” model (right) was not correct (credit: Sandy Simon, The Rockefeller University)

Scientists at Rockefeller University have developed a new polarized microscopy technique that measures how components of large protein complexes are arranged in relation to one another.

“Our new technique allows us to measure how components of large protein complexes are arranged in relation to one another,” says Sandy Simon, head of the Laboratory of Cellular Biophysics. “This has the potential to give us important new information about how the nuclear pore complex functions, but we believe it can also be applied to other multi-protein complexes such as those involved in DNA transcription, protein synthesis or viral replication.”

The scientists genetically attached fluorescent markers to individual components of the nuclear pore complex, a huge cluster of proteins that serves as a gateway to a cell’s nucleus.  They then replaced the cell’s own copy of the gene that encodes the protein with the new form that has the fluorescent tag.

The scientists used the technique to study nuclear pore complexes in both budding yeast and human cells. In the case of the human cells, their new data showed that multiple copies of a key building block of the nuclear pore complex, the Y-shaped subcomplex, are arranged head-to-tail, rather than like fence posts, confirming a model proposed in 2007.

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