Welcome to my talk.
My name is Keith Willison.
I'm a professor of chemistry at Imperial College London,
where I've worked for the past decade or so.
Much of the work on the chaperonin that's I'm going to talk to you today
about was performed during my 30 years at the Institute of Cancer Research,
where I pioneered the genetics and biochemical analysis of this fascinating system.
I've always maintained that the main function of
this molecular assembly is to fold the cytoskeletal proteins,
actin, and tubulin, and that's everything else,
all sorts of ancillary functions.
This machinery, unlike the bacterial system GroEL,
which I'll mention in a moment,
is a completely specific machine for folding a relatively small number of proteins,
and that's one of the major points I'd like to get across today.
This talk that I'm giving now is an updated version of
my original HSTalks which I wrote in 2007.
Now much of our work on CCT since then,
which has been published in many technical papers during the past decade or so,
has been recently reviewed and a pair of articles that I've written.
One in the Biochemical Journal,
one as a symposium proceedings in the Philosophical Transactions of the Royal Society.
The Biochemical Journal paper is really about mechanism,
structural studies and evolution whereas the fill trends
paper really discusses the substrate specificity of
this eukaryotic cytosolic chaperonin and also outlines
my model for the role of this chaperonin in regulating cell size,
cell growth, and cell cycle control.
Now, this talk is going to be fairly high level and general.
Although obviously I need to convey some technical information,
but I just really want to hopefully help listeners to see where
the field is at the moment and what some of the outstanding problems
are that need addressing and also why it's
a really exciting system to try and understand some really deep problem in
evolution of eukaryotic cells and also in
the control of many signaling pathways in addition to the cell cycle.