Keeping the lid on destruction

irst there was green fluorescent protein (GFP) from jellyfish, then came red fluorescent protein (DsRed) from coral. Now researchers from the University of California at Irvine show that DsRed may become equally indispensable for tracking cells, organelles, and fusion proteins by turning them... green? Ian Parker says he and his colleagues made the discovery quite by accident while exploring the use of DsRed for multiphoton confocal imaging. Brief exposure to a femtosecond-pulsed laser beam turned DsRed's fluorescence from F DsRed-expressing cells before (upper) and after (lower) " greening " of the cyto-plasm (left) or nucleus (right). Keeping the lid on destruction roteins slated for destruction enter the proteasome core particle (CP) through a channel that usually remains closed for safety's sake. It opens when a CP associates with the proteasome regulatory particle (RP), which recognizes the substrates and ushers them into the channel. What persuades the channel to open? A ring of six ATPases straddles the channel, and those enzymes have been thought to figure in this process. Now, Alwin Köhler and his colleagues in the laboratories of Daniel Finley and Alfred Gold-berg (Harvard Medical School, P Rpt2 (top and bottom) controls access to enzymes in the proteasome core. Boston, MA) report, surprisingly, that just one of the six ATPases, Rpt2, is the key that unlocks the channel. In addition, the products of protein degradation exit the proteasome the same way that they came in, pointing to some possible traffic problems. The paper also reports on one reason why the proteasome might want to keep tight control over gating. With the help of yeast CP mutants that stay open, the authors compared the products of the proteasome when it was kept in a closed or an open state. The median length of peptides produced by the mutant CP was 40% larger than those produced by the wild type. The results, Finley says, confirmed their suspicions that the size of products is determined by competition between their ongoing degradation and their exit from the internal chamber of the proteasome. The size of degradation products is not an idle question, because in mammals such a product may be incorporated into a class I histocompatibility molecule to be presented to the immune system as a potential antigen. Therefore, proteasome efficiency is likely to be important for immune system function. That makes the state of the channel important too, and may explain why the …