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Date:10/24/2013

lymerase II. When they determined its 3-dimensional structure, the scientists found that some of the 'extra' modules in RNA polymerase I are remarkably similar to other, separate proteins that RNA polymerase II needs to do its job. It seems that RNA polymerase I has brought those helper modules permanently on board. In another part of the molecule, Mller and colleagues found that RNA polymerase I appears to have combined what in RNA polymerase II are two separate modules into a single, multi-tasking component. Together, these changes likely explain why RNA polymerase I can produce RNA molecules at a faster rate than RNA polymerase II.

The findings also imply that the cell has fewer ways of controlling RNA polymerase I's activity, since it can't influence it by changing the availability of helper proteins as it does in the case of RNA polymerase II. But here, too, RNA polymerase I's Swiss-army knife strategy provides a solution. The structure showed that this molecular machine has a built-in regulatory mechanism: it can stop itself from attaching to DNA by bending a loop in its structure to block the space the DNA would usually dock onto.


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Contact: Sonia Neves
sonia.furtado@embl.de
European Molecular Biology Laboratory
Source:Eurekalert  

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