Annual Robert Ross lecture, Thursday, March 21, 1-2:30, Karolin Luger

[Ralf Bundschuh]

Dear Physics colleagues,

Next Thursday (3/21), the Biophysics program will hold its annual Robert 
Ross lecture.  This is the major event in our academic year.  This 
year's speaker is Karolin Luger from the University of Colorado, 
Boulder, a world expert in nucleosome structure and excellent speaker. 
She will speak on:

     Adventures in the chromatin jungle:
     Nucleosome evolution and interactions

at

   Thursday, March 21, 1-2:30, Davis Heart and Lung Institute 170

and you are cordially invited to attend.

Graduate students are also encouraged to stay after the talk in DHLRI 
159 to meet with the speaker (refreshments provided).

A flier is attached.

    Yours
          Ralf

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Robert Ross Lecture, Thursday, March 21, 1-2:30, DHLRI170
Karolin Luger, University of Colorado, Boulder

Adventures in the chromatin jungle:
Nucleosome evolution and interactions

Invariably, all eukaryotes organize their DNA into nucleosomes, 
consisting of an octamer of the four core histone proteins H2A, H2B, H3, 
and H4, around which 147 base pairs of DNA are wrapped in two tight 
superhelical turns. With the discovery of small histone-like proteins in 
most known Archaea, the likely origin of this fold was identified. Most 
Archaea encode only one or two minimal histones that form polymers 
around which DNA coils in a quasi-continuous superhelix rather than 
forming defined particles. I will discuss implications of this discovery 
for the evolutionary origins of eukaryotic chromatin.

Nucleosomes are highly abundant, and all nuclear factors have to operate 
in this structural context. Poly(ADP-ribose) polymerase 1 (PARP1) and 
the less abundant PARP2 together are essential for the DNA damage repair 
response in all eukaryotic cells. PARP1 and PARP2 bind tightly to 
chromatin and nucleosomes, yet are rapidly recruited to sites of DNA 
damage. Using live-cell imaging coupled with mathematical modeling, we 
studied the rapid recruitment of PARP1 to sites of DNA damage in vivo.
Combined with millisecond timescale measurements of DNA binding to PARP1 
in vitro, we arrived at a mechanism for PARP1 movement in the nucleus.
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