TY - JOUR
T1 - PUPylation
T2 - something old, something new, something borrowed, something Glu
AU - DeMartino, George N.
N1 - Funding Information:
Work in our laboratory is supported by grants from the National Institutes of Health (DK 46181; www.nih.gov ) and the Welch Foundation (I-500; www.welch1.org ). I thank Thomas Gillette, Brajesh Kumar, Kim Orth, Sohini Mukherjee and anonymous reviewers for helpful comments.
PY - 2009/4
Y1 - 2009/4
N2 - Most eukaryotic proteins are degraded by the 26S proteasome as a consequence of their covalent modification with ubiquitin. Although the proteasome is found in some prokaryotes, ubiquitin is not, which indicates that substrates are targeted to prokaryotic proteasomes by a fundamentally different mechanism. A recent study has identified Pup (prokaryotic ubiquitin-like protein) as a mycobacterial protein that functions in a manner analogous to ubiquitin for proteasome-dependent proteolysis in prokaryotes.
AB - Most eukaryotic proteins are degraded by the 26S proteasome as a consequence of their covalent modification with ubiquitin. Although the proteasome is found in some prokaryotes, ubiquitin is not, which indicates that substrates are targeted to prokaryotic proteasomes by a fundamentally different mechanism. A recent study has identified Pup (prokaryotic ubiquitin-like protein) as a mycobacterial protein that functions in a manner analogous to ubiquitin for proteasome-dependent proteolysis in prokaryotes.
UR - http://www.scopus.com/inward/record.url?scp=63549093793&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=63549093793&partnerID=8YFLogxK
U2 - 10.1016/j.tibs.2008.12.005
DO - 10.1016/j.tibs.2008.12.005
M3 - Short survey
C2 - 19282181
AN - SCOPUS:63549093793
SN - 0968-0004
VL - 34
SP - 155
EP - 158
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 4
ER -