BOSTON In molecular biology, the ribosome represents the machinery necessary to assemble proteins, the building blocks of life. In this process, information encoded in the genome's DNA is first transcribed to messenger RNA in the nucleus, then transported to the ribosome where protein-assembly instructions are put in motion to translate the code into actual proteins.
But in recent years, it has been demonstrated that the ribosome is far more than just a processing unit; indeed, current research points to an important role for this complex structure in actively regulating biological processes.
Now, in a first-of-its-kind study that broadly examines the composition of the riboproteome, a scientific team led by investigators at Beth Israel Deaconess Medical Center (BIDMC) reveals previously unappreciated components of the ribosome, uncovering a large and dynamic structure that, among other things, can be altered in cancer. Published in today's on-line issue of the journal Cell Reports, the study additionally describes the development of an analytic platform that can be widely applied to numerous biological systems to highlight the functional roles of possible disease genes associated with the riboproteome.
"A primary goal of our lab is to gain a better understanding of translation and its impact on cancer," explains senior author Pier Paolo Pandolfi, MD, PhD, Scientific Director of the Cancer Center at BIDMC and George C. Reisman Professor of Medicine at Harvard Medical School (HMS). "So a key focus of our work has been the role of the ribosome. While the conventional wisdom has been that ribosome composition is absolutely fixed, we have recently pursued the hypothesis that it is, in fact, flexible and dynamic. Moreover, it has become apparent during the course of our investigations that the functional deregulation of the ribosome is implicated in disease initiation and progression, and could serve as a potential target for ther
|Contact: Bonnie Prescott|
Beth Israel Deaconess Medical Center