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BEGIN:VEVENT
UID:DSC-15652
DTSTART;TZID=Europe/Berlin:20190305T110000
SEQUENCE:1551830814
TRANSP:OPAQUE
DTEND;TZID=Europe/Berlin:20190305T120000
URL:https://www.dresden-science-calendar.de/calendar/en/detail/15652
LOCATION:MPI-CBG\, Pfotenhauerstraße 10801307 Dresden
SUMMARY:Cernohorska: C-terminal tail of tubulin mediate assembly of flagell
 ar microtubule doublet in vitro
CLASS:PUBLIC
DESCRIPTION:Speaker: Marketa Cernohorska\nInstitute of Speaker: Institute o
 f Molecular Genetics of the ASCR\, v. v. i.\, Prague\, Czech Republic\nTop
 ics:\nBiologie\n Location:\n  Name: MPI-CBG (MPI-CBG Galleria)\n  Street: 
 Pfotenhauerstraße 108\n  City: 01307 Dresden\n  Phone: +49 351 210-0\n  F
 ax: +49 351 210-2000\nDescription: In centriole\, microtubules are assembl
 ed in conserved structure of nine-fold blades in triplets (A\, B\, C-micro
 tubule) that elongates as doublets (A\, B-microtubule) to the axoneme and 
 provide scaffold for intraflagellar transport. While tough structure of th
 ese blades has long been known\, the mechanism by which they form remained
  unknown. The most recent work on flagellar doublets using cryo-electron t
 omography (Ichikawa et al.\, 2017) suggested two possible hypotheses. Firs
 t\, B-microtubule is bound to A-microtubule via small microtubule inner pr
 oteins penetrating through the microtubule wall\, and second\, both microt
 ubules might be bound directly via unique side-to-side contacts. In order 
 to reveal the nature and mechanism of microtubule doublet assembly\,  I em
 ployed a cell-free assay combined with limited proteolytic digestion. This
  approach showed for the first time that microtubule doublet is assembled 
 solely from tubulin. In this talk I will explain our discovery with Paul G
 uichard and Virginie Hamel of the inhibitory role of tubulin C-terminus. I
 n addition\, I will show my recent project which aims to reveal BBSome ass
 embly using novel technique of expansion microscopy.
DTSTAMP:20260528T051305Z
CREATED:20190209T000740Z
LAST-MODIFIED:20190306T000654Z
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