TY - JOUR
T1 - Light-mediated inhibition of protein synthesis
AU - Goard, Michael
AU - Aakalu, Girish
AU - Fedoryak, Olesya D.
AU - Quinonez, Carlo
AU - St. Julien, Jamii
AU - Poteet, Stephen J.
AU - Schuman, Erin M.
AU - Dore, Timothy M.
N1 - Funding Information:
This research was supported by the Howard Hughes Medical Institute, the National Institutes of Health (MH065537, E.M.S.), the University of Georgia Research Foundation, an award from the Research Corporation (T.M.D.), and a University of Georgia Thomas Whitehead Scholarship in Chemistry for summer research (S.J.P.). The authors would like to thank Procter & Gamble for a generous donation of anisomycin and Kenneth A. Miller and Rebekah L. Rogers for technical assistance.
PY - 2005
Y1 - 2005
N2 - The regulation of protein synthesis is vital for a host of cell biological processes, but investigating roles for protein synthesis have been hindered by the inability to selectively interfere with it. To inhibit protein synthesis with spatial and temporal control, we have developed a photo-releasable anisomycin compound, N-([6-bromo-7-hydroxycoumarin-4-yl]methyloxycarbonyl) anisomycin (Bhc-Aniso), that can be removed through exposure to UV light. The area of protein synthesis inhibition can be restricted to a small light-exposed region or, potentially, the volume of two-photon excitation if a pulsed IR laser is the light source. We have tested the compound's effectiveness with an in vitro protein-translation system, CHO cells, HEK293 cells, and neurons. The photo-released anisomycin can inhibit protein synthesis in a spatially restricted manner, which will enable the specific inhibition of protein synthesis in subsets of cells with temporal and spatial precision.
AB - The regulation of protein synthesis is vital for a host of cell biological processes, but investigating roles for protein synthesis have been hindered by the inability to selectively interfere with it. To inhibit protein synthesis with spatial and temporal control, we have developed a photo-releasable anisomycin compound, N-([6-bromo-7-hydroxycoumarin-4-yl]methyloxycarbonyl) anisomycin (Bhc-Aniso), that can be removed through exposure to UV light. The area of protein synthesis inhibition can be restricted to a small light-exposed region or, potentially, the volume of two-photon excitation if a pulsed IR laser is the light source. We have tested the compound's effectiveness with an in vitro protein-translation system, CHO cells, HEK293 cells, and neurons. The photo-released anisomycin can inhibit protein synthesis in a spatially restricted manner, which will enable the specific inhibition of protein synthesis in subsets of cells with temporal and spatial precision.
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U2 - 10.1016/j.chembiol.2005.04.018
DO - 10.1016/j.chembiol.2005.04.018
M3 - Article
C2 - 15975514
AN - SCOPUS:23144442313
VL - 12
SP - 685
EP - 693
JO - Cell Chemical Biology
JF - Cell Chemical Biology
SN - 2451-9448
IS - 6
ER -