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.com
Volume 3, Issue 2
ISSN: 2470-9905
Crystallography 2017
October 16-17, 2017
2
nd
International Conference on
October 16-17, 2017 | Chicago, USA
Applied Crystallography
Structural diversity and similarity among Clp chaperones from plants and mycobacteria
Dileep Vasudevan, Manas Kumar Jagdev
and
Chinmayee Mohapatra
Institute of Life Sciences, India
U
nfolded or damaged proteins in a cell usually get targeted for degradation before they start accumulating and reach toxic levels.
In bacteria as well as plants, chaperones and proteases perform a major role in this important protective and restorative function.
Caseinolytic protease-associated chaperone C1 (ClpC1) is one such protein that performs the function of cellular protein quality
control, primarily through its association with ClpP1P2 protease core in mycobacteria, wherein the chaperone aids in ATP-dependent
unfolding of protein substrates to be degraded by the protease machinery. In case of plants, they have the Clp chaperones ClpC1 and
ClpC2 which associate with a similar protease core - ClpPR, all within the chloroplast stroma. In addition, plants have an additional
stromal chaperone called ClpD which also associates with Clp protease. ClpC and ClpD proteins belong to the family of AAA+
HSP100 proteins. Both are functional as hexamers and have a 3-domain organization wherein the N-terminal domain is mostly
involved in substrate recognition and the middle and C-terminal domains are with ATPase activity, aiding substrate unfolding.
Crystal structures reveal the N-terminal domain of ClpC1 from
M. tuberculosis
and
A. thaliana
to be very similar in organization;
however, the plant specific AtClpD has a structural organization quite different from any known Clp chaperones that have been
characterized so far. Herein, we discuss the findings from our structural studies on Clp chaperone proteins from
Mycobacterium
and
Arabidopsis.
dileep@ils.res.inStruct Chem Crystallogr Commun, 3:2
DOI: 10.21767/2470-9905-C1-003