Speaker
Gregor Hagelueken
(University of Bonn)
Description
We report the crystal structure of CRISPR-Lon, a type-III CRISPR related protease that is activated by cyclic oligoadenylates. The protein is a soluble monomer and contains a SAVED domain that accommodates cA4. Further, we show that CRISPR-Lon forms a stable complex with the 34 kDa CRISPR-T protein. Upon activation by cA4, CRISPR-Lon specifically cleaves CRISRP-T, releasing CRISPR-T23, a 23 kDa fragment that is structurally very similar to MazF toxins and is likely a sequence specific nuclease.
Primary authors
Christophe Rouillon
(University of Bonn)
Niels Schneberger
(University of Bonn)
Haotian Chi
(University of St Andrews)
Martin Peter
(University of Bonn)
Matthias Geyer
(University of Bonn)
Wolfgang Boenigk
(3Center of Advanced European Studies and Research (caesar))
Reinhard Seifert
(3Center of Advanced European Studies and Research (caesar))
Malcolm White
(University of St Andrews)
Gregor Hagelueken
(University of Bonn)
