Protein oligomerization
in Aleuria aurantia lectin family – importance and difficulties
Josef Houser1,2, Jan Komárek2,
Nikola Kostlánová1, Gianluca Cioci4, Anne Imberty5,
Michaela Wimmerová1,2,3
1Central
European Institute of Technology, Masaryk University, Kamenice
5, 625 00 Brno, Czech Republic, 2National Centre for Biomolecular Research and 3Department of
Biochemistry, Faculty of Science, Masaryk University, Kotlářská
2, 611 37 Brno, Czech Republic
4European Synchrotron Radiation Facility,
6 rue Jules Horowitz, 38043 Grenoble, France
5CERMAV-CNRS,
BP53, 38041 Grenoble Cedex 9, France
The formation of quaternary structure is
crucial for function of many different proteins. Many of them are fully
functional only upon oligomerization or change their
properties due to binding of several subunits to each other. The determination
of protein oligomeric state is important to fully describe
its structural and functional properties. Combination of several
methods like size-exclusion chromatography, dynamic light scattering or
analytical ultracentrifugation together with X-ray crystallography enable
us to see deeper into protein complexity.
Oligomerization and multivalency are very important for
carbohydrate binding proteins, lectins, responsible
among others for pathogen binding to host tissues. In some cases the binding
sites are formed in between two subunits. In the Aleuria aurantia lectin
family, oligomerization plays role in two different
ways. Whereas bacterial lectins like RSL from Ralstonia solanacearum [1]
or BambL from Burkholderia ambifaria [2] form trimers to
establish complete β-propeller fold, eucaryotic lectins like AAL from Aleuria aurantia [3] or AFL from Aspergillus fumigatus
combine two β-propellers to further increase avidity effect. In addition,
although the terciary structures of these proteins
are very similar, there are interesting differences in dimerization.
Detail knowledge in this area can help us to design highly efficient artificial
lectins, as well as improve the treatment strategy in
cases, where lectins play integral role in infection
process.
This
work was supported by Ministry of Education of
the Czech Republic (ME08008),
Grant Agency of the Czech Republic (303/09/1168), the
European Community's Seventh
Framework Program under the
"Capacities" specific
programme (Contract No. 286154) and CEITEC - Central
European Institute of Technology with
research infrastructure supported by the
project CZ.1.05/1.1.00/02.0068 from
European Regional Development Fund.
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