Übersicht
colloquia - [ 19.01.2009 (11.00) ]
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"Molecular mechanisms of chaperone machines"
Sprecher: Prof. Bernd Bukau, Zentrum für Molekulare Biologie der Universität Heidelberg
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The ensemble of molecular chaperones constitutes the cellular system
that assists folding and assembly of newly synthesized proteins,
translocation of unfolded proteins across membranes, as well as
refolding and degradation of misfolded and aggregated proteins. In the
E. coli cytosol, the ribosome-associated chaperone Trigger Factor
interacts with short nascent polypeptide chains and assists early
folding steps. The major Hsp70 chaperone, DnaK, uses the energy of ATP
and the assistance by the DnaJ and GrpE co-chaperones to fold newly
synthesized proteins and refold misfolded proteins. DnaK furthermore
cooperates with the AAA+ ATPase, ClpB, to solubilize and refold
aggregated proteins. The remarkable remodeling activity of ClpB is
essential for cell survival under severe heat stress. A closely related
AAA chaperone. The structurally related AAA protein, ClpA, forms the
chaperone subunit of the ClpA-ClpP protease, which cooperates with the
adaptor protein ClpS in targeting N-terminally tagged proteins of the
N-end rule pathway to regulated proteolysis. This seminar will describe
our current knowledge of the working mechanisms of these chaperones.
http://www.zmbh.uni-heidelberg.de/Bukau/default.shtml
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Ort:
Carl-Bosch-Auditorium des Studios der Villa Bosch, 69118 Heidelberg, Schloss-Wolfsbrunnenweg 33 (Eingang Studio - ca. 100 m vom Eingang zur Villa Bosch entfernt, auf der Talseite des Schloss-Wolfsbrunnenweges; Näheres zur Anfahrt siehe unter www.studio.villa-bosch.de.
Parken:
Tiefgarage „Unter der Boschwiese“ (unentgeltlich).
Contact:
Bärbel Mack
EML Research gGmbH
Schloss-Wolfsbrunnenweg 33
69118 Heidelberg
Phone: +49 (0)6221 - 533 - 201
Fax: +49 (0)6221 - 533 - 298
Email: [email protected]
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