Plant Chaperones Lab

1
Plant Chaperones Lab ??????? ??????
Prof. Adina Breiman????' ????? ?????
517, Britania, Tel [phone] (office),
03-6409845 (lab) adina_at_post.tau.ac.ilhttp//www.t
au.ac.il/lifesci/plant_sciences/USR/breiman/
Our studies are focused on the study of the
family of co chaperones with the enzymatic
activity of peptidyl prolyl cis trans isomerases
(PPIases) in plants.This large family possess
several families the cyclophilins ,FKBPs and
parvulins.Members of these families were shown to
play important roles in signal transduction and
protein folding due to their activity as
chaperones and PPIases. We chose to work on the
FKBP family because members of this have
important roles in signal transduction in mammals
and yeast. The FKBP family is highly conserved
among all organisms and after studying two
members of this family in wheat , we have
switched to the Arabidopsis system because of the
big genetic potential of Arabidopsis mutants and
genomics. We study members of the FKBP family
which are heat shock proteins, bind the heat
shock protein HSP90 ,calmodulin and dynein. By
using mutants missing the FKBP genes Rof1 and Rof
2 and by over expressing those genes we plan to
understand their role in signal transduction and
molecular chaperone activity. Recent
Publications Kurek, I., R. Dulberger, D.
Sudhakar, P. Christou A. Breiman, 2002.
Deletion of the C terminal 138 amino acids
abrogates calmodulin binding, dimerisation and
male fertility in transgenic rice. Plant Mol.Biol
.48, 369-381. Kurek I., F. Pirkl, E.Fischer, J.
Buchner A. Breiman, 2002. The wheat FKBP73
functions in vitro as a molecular chaperone
independent of its peptidyl prolyl cis -trans
isomerase activity. Planta 215,119-126. Kurek. I
, E. Stoger, R. Dulberger, P. Christou A
.Breiman 2002.Over expression of the wheat FKBP77
and the heat induced FKBP77 in the transgenic
wheat reveals different function of the two
isoforms Transgenic Research 11,373-379.
Graduate Students Samuel Bocovsa Ruth
Wilunsky Yulia Skovorodnikov