"Structures
of the bacterial ribosome and the mechanism of translocation"
Presented by Jamie Cate
University of Califonia-Berkeley
The ribosome is the universally conserved cellular machine
that translates the genetic code into proteins.
Protein biosynthesis requires many large-scale rearrangements in the
ribosome as each amino acid is added to a growing polypeptide chain. A key conformational change in the ribosome
that is essential for translation is rotation of the small ribosomal subunit
relative to the large subunit. Rotation
of the ribosomal subunits occurs in all stages of translation–initiation,
elongation, termination, and ribosome recycling–and is targeted by clinically
useful antibiotics. In addition to
rotation of the two ribosomal subunits, large-scale movements of the head
domain of the small ribosomal subunit are thought to control the movement of
mRNA and tRNAs as they traverse the three tRNA binding sites within the
ribosome, a process termed translocation.
As with subunit rotation, movement of the head domain is a target for
clinically useful antibiotics. I will
present structures of the 70S ribosome from Escherichia
coli that reveal new aspects of the molecular basis for subunit rotation
and movement of the head domain of the small subunit. In bacteria, the ribosome
is targeted by numerous antibiotics, which affect many steps in protein
synthesis. I will also present structures of the ribosome with antibiotics
bound that shed light on how these compounds inhibit specific steps of the
translocation mechanism.
Hosted by Prof. Ruben Gonzalez
Thursday, April 29, 2010
Meet the speaker at 1:30pm in room 328 Havemeyer
Tea & cookies at 4:00pm in room 328 Havemeyer
Seminar at 4:30pm in room 209 Havemeyer
