THE ROLE OF QUARTERNARY STRUCTURE IN FLUORESCENT PROTEIN STABILITY
Olesia V. Stepanenko,1 V. V. Verkhusha,2,3 M. M. Shavlovsky,4
T. D. Aleinikova,4
V. N. Uversky,5,6 I. M. Kuznetsova,1 K. K. Turoverov 1
1 Institute of Cytology, RAS, St. Petersburg, Russia,
2 Center for Molecular Medicine, Moscow State University, Russia,
3 University of Colorado Health Science Center, Denver, Colorado, USA,
4 Institute for Experimenal Medicine RAMS, St. Petersburg, Russia,
5 Institute for Biological Instrumentation RAS, Pushchino, Russia,
and 6 University of Indianapolis, Indiana, USA;
1 e-mail: kkt@mail.cytspb.rssi.ru
The stability of fluorescent proteins (FPs) is of great importance for their use as reporters in studies of gene
expression, protein dynamics and localization in cell. A comparative analysis of conformational stability of fluorescent proteins,
having different association state was done. The list of studied proteins includes EGFP (monomer of green fluorescent protein,
GFP), zFP506 (tetramer GFP), mRFP1 and "dimer2" (monomer and dimmer of red fluorescent protein), DsRed1 (red tetramer). The
character of fluorescence intensity changes induced by guanidine hydrochloride (GdnHCl) of these proteins differs significantly.
Green tetramer zFP506 has been shown to be more stable than green monomer EGFP, red dimmer "dimer2" has been shown to be less
stable than red tetramer DsRed1, while red monomer mRFP1 has been shown to be practically as stable as tetramer DsRed1. It is
concluded that the quaternary structure, being an important stabilizing factor, does not represent the only circumstance dictating
the dramatic variations between fluorescent proteins in their conformational stability.
Key words: fluorescent proteins, oligomerization, protein stability, protein folding
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