The smooth and efficient functioning of any system necessarily requires a mechanism for recognizing and removing components that have served their purpose and are no longer needed, in order to make way for ones that are. It's waste disposal, and at the cellular level it's the important activity of proteasomes that maintain cellular health by identifying and degrading proteins that have been targeted as obsolete or damaged. (To put this in perspective, consider that at any given moment a human cell typically contains about 100,000 different proteins.) This housekeeping function of proteasomes is critical to a broad range of vital biochemical processes, including transcription, DNA repair, and the immune defense system. Since the proteasome process was only first described in 2004 (by Nobel Prize-winning chemists), our understanding of its mechanics has been limited.
Now, cell biology research scientists at the University of California Berkeley and Lawrence Berkeley Lab have discovered a way to examine the complete architecture of the proteasome regulatory particle at a subnonometer scale. Biophysicist Eva Nogales, the research team’s co-principal investigator, describes their findings in a recent issue of Nature. The breakthrough was accomplished using electron microscopy, image analysis, and a 'revolutionary new system for protein expression' developed by her colleague and co-PI, biochemist Andreas Martin. Nogales says this of Martin's contribution:
“Until now researchers had to work with purified protein complexes from the cell, which could not be manipulated or modified in any way. Andy Martin’s new heterologous expression system allows for the manipulation and dissection of protein functions."
What the team found when they were able to look inside the protease regulatory system was a clearer picture of "the mechanisms underlying proteasomal substrate degradation, the irreversible and hence critical step for the unidirectional control of cellular pathways," according to Martin. He also says of the research that it "opens the possibility of manipulating proteasome activity for the treatment of cancer and other diseases.”
The Lawrence Berkeley National Laboratory (LBL, LBNL, or simply Berkeley Lab) sits on a 200-acre parcel adjacent to the UC Berkeley campus and is managed by UCB for the DOE's Office of Science. LBL employs approximately 4,200 scientists, engineers, support staff and students. Its budget for 2011 was $836 million. LBL is currently planning a major consolidation of its biosciences program with a new facility to be constructed on its waterfront property in nearby Richmond, California. The Richmond complex will allow LBL to grow while maintaining its ties to the UC Berkeley campus.
In case you missed our last UCB/LBNL blog yesterday, in conjunction with Big Data, read it here!
Biotechnology Calendar, Inc. will be holding its 15th Annual Berkeley BioResearch Product Faire™ event on the UCB campus on June 6, 2012. This networking opportunity brings life science researchers together with laboratory equipment suppliers to discuss the latest technologies in lab science. For information on exhibiting, click below:
If you are interested in attending the UC Berkeley event register here.