*Post-doc position available, from Jan 2008*
*Title : *Crystallography of /B. subtilis/ ribonucleases
*Group :* Ciarán Condon, under supervision of Inés Li de la Sierra-Gallay.
*Address :* CNRS UPR9073/IFR550, Institut de Biologie Physico-Chimique,
13 rue Pierre et Marie Curie, 75005 Paris.
*Contact :* [EMAIL PROTECTED] <mailto:[EMAIL PROTECTED]>_ or
[EMAIL PROTECTED] <mailto:[EMAIL PROTECTED]>_
*Web-site :* http://www.ibpc.fr/UPR9073/condon/index_en.html
*Financed by :* Agence Nationale de la Recherche (ANR) for 2 years
*Description :* It has recently become clear/ /that the pathways of RNA
maturation and decay in the Gram-positive bacterium /B. subtilis/ are
very different from those of the generally accepted bacterial paradigm,
the Gram-negative /E. coli/. As such, /B. subtilis/ is a rich source of
new bacterial ribonucleases. We have recently solved the crystal
structure of one of these : RNase Z, both free and in complex with its
tRNA product (Li de la Sierra-Gallay et al., 2006; Li de la
Sierra-Gallay et al., 2005). We now hope to persue this study with other
recently identified /B. subtilis/ RNases and their substrates. Among
these are the 5S rRNA maturase RNase M5, the 23S rRNA maturase YazC, and
the 3’ to 5’ exoribonuclease KapD. We would like to solve the crystal
structures of RNase Z in complex with its precursor (rather than
product) species and that of the endo/exoribonuclease RNase J1 in
complex with RNA.
Candidates should have some experience in protein purification,
crystallography and structure resolution.
*References :*
Li de la Sierra-Gallay, I., Mathy, N., Pellegrini, O. and Condon, C.
(2006) Structure of the ubiquitous 3' processing enzyme RNase Z bound to
transfer RNA. /Nat Struct Mol Biol/, *13*, 376-377.
Li de la Sierra-Gallay, I., Pellegrini, O. and Condon, C. (2005)
Structural basis for substrate binding, cleavage and allostery in the
tRNA maturase RNase Z. /Nature/, *433*, 657-661.
--
Ines Gallay
CNRS FRC550
Institut de Biologie Physico-Chimique
13 rue Pierre et Marie Curie
75005 Paris
FRANCE
e-mail: [EMAIL PROTECTED]
