Rhizobium etli CFN42 is a symbiotic nitrogen-fixing bacterium of the common bean Phaseolus vulgaris. The symbiotic plasmid p42d of R. etli comprises a gene encoding a putative (strept)avidin-like protein, named rhizavidin. The amino acid sequence identity of rhizavidin in relation to other known avidin-like proteins is 20–30%. The amino acid residues involved in the (strept)avidin–biotin interaction are well conserved in rhizavidin. The structural and functional properties of rhizavidin were carefully studied, and we found that rhizavidin shares characteristics with bradavidin, streptavidin and avidin. However, we found that it is the first naturally occurring dimeric protein in the avidin protein family, in contrast with tetrameric (strept)avidin and bradavidin. Moreover, it possesses a proline residue after a flexible loop (GGSG) in a position close to Trp-110 in avidin, which is an important biotin-binding residue. [3H]Biotin dissociation and ITC (isothermal titration calorimetry) experiments showed dimeric rhizavidin to be a high-affinity biotin-binding protein. Its thermal stability was lower than that of avidin; although similar to streptavidin, it was insensitive to proteinase K. The immunological cross-reactivity of rhizavidin was tested with human serum samples obtained from cancer patients exposed to (strept)avidin. No significant cross-reactivity was observed. The biodistribution of the protein was studied by SPECT (single-photon emission computed tomography) imaging in rats. Similarly to avidin, rhizavidin was observed to accumulate rapidly, mainly in the liver. Evidently, rhizavidin could be used as a complement to (strept)avidin in (strept)avidin–biotin technology.
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August 2007
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Research Article|
July 13 2007
Rhizavidin from Rhizobium etli: the first natural dimer in the avidin protein family
Satu H. Helppolainen;
Satu H. Helppolainen
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
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Kirsi P. Nurminen;
Kirsi P. Nurminen
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
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Juha A. E. Määttä;
Juha A. E. Määttä
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
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Katrin K. Halling;
Katrin K. Halling
†Department of Biochemistry and Pharmacy, Åbo Akademi University, Tykistökatu 6, FI-20520 Turku, Finland
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J. Peter Slotte;
J. Peter Slotte
†Department of Biochemistry and Pharmacy, Åbo Akademi University, Tykistökatu 6, FI-20520 Turku, Finland
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Tuulia Huhtala;
Tuulia Huhtala
‡Department of Chemistry, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland
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Timo Liimatainen;
Timo Liimatainen
‡Department of Chemistry, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland
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Seppo Ylä-Herttuala;
Seppo Ylä-Herttuala
§A.I. Virtanen Institute, Department of Molecular Medicine and Biotechnology, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland
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Kari J. Airenne;
Kari J. Airenne
§A.I. Virtanen Institute, Department of Molecular Medicine and Biotechnology, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland
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Ale Närvänen;
Ale Närvänen
‡Department of Chemistry, University of Kuopio, P.O. Box 1627, FI-70211 Kuopio, Finland
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Janne Jänis;
Janne Jänis
∥Department of Chemistry, University of Joensuu, P.O. Box 111, FI-80101 Joensuu, Finland
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Pirjo Vainiotalo;
Pirjo Vainiotalo
∥Department of Chemistry, University of Joensuu, P.O. Box 111, FI-80101 Joensuu, Finland
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Jarkko Valjakka;
Jarkko Valjakka
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
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Markku S. Kulomaa;
Markku S. Kulomaa
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
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Henri R. Nordlund
Henri R. Nordlund
1
*Institute of Medical Technology, University of Tampere, FI-33014 Tampere, Finland
1To whom correspondence should be addressed, at the present address NEXT Biomed Technologies Oy, Viikinkaar, 4, Fl-00790 Helsinki, Finland (email [email protected]).
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Publisher: Portland Press Ltd
Received:
January 12 2007
Revision Received:
March 19 2007
Accepted:
April 20 2007
Accepted Manuscript online:
April 20 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem J (2007) 405 (3): 397–405.
Article history
Received:
January 12 2007
Revision Received:
March 19 2007
Accepted:
April 20 2007
Accepted Manuscript online:
April 20 2007
Citation
Satu H. Helppolainen, Kirsi P. Nurminen, Juha A. E. Määttä, Katrin K. Halling, J. Peter Slotte, Tuulia Huhtala, Timo Liimatainen, Seppo Ylä-Herttuala, Kari J. Airenne, Ale Närvänen, Janne Jänis, Pirjo Vainiotalo, Jarkko Valjakka, Markku S. Kulomaa, Henri R. Nordlund; Rhizavidin from Rhizobium etli: the first natural dimer in the avidin protein family. Biochem J 1 August 2007; 405 (3): 397–405. doi: https://doi.org/10.1042/BJ20070076
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