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Originally published In Press as doi:10.1074/jbc.M212007200 on February 4, 2003

J. Biol. Chem., Vol. 278, Issue 15, 12977-12984, April 11, 2003
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Transition from Natively Unfolded to Folded State Induced by Desiccation in an Anhydrobiotic Nematode Protein*

Kshamata GoyalDagger , Laurence TisiDagger , Amrik BasranDagger §, John Browne, Ann Burnell, Jesús Zurdo||, and Alan TunnacliffeDagger **

From the Dagger  Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, United Kingdom, the  Institute of Bioengineering and Agroecology, Department of Biology, National University of Ireland Maynooth, Maynooth, County Kildare, Ireland, and the || Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom

Late embryogenesis abundant (LEA) proteins are associated with desiccation tolerance in resurrection plants and in plant seeds, and the recent discovery of a dehydration-induced Group 3 LEA-like gene in the nematode Aphelenchus avenae suggests a similar association in anhydrobiotic animals. Despite their importance, little is known about the structure of Group 3 LEA proteins, although computer modeling and secondary structure algorithms predict a largely alpha -helical monomer that forms coiled coil oligomers. We have therefore investigated the structure of the nematode protein, AavLEA1, in the first such analysis of a well characterized Group 3 LEA-like protein. Immunoblotting and subunit cross-linking experiments demonstrate limited oligomerization of AavLEA1, but analytical ultracentrifugation and gel filtration show that the vast majority of the protein is monomeric. Moreover, CD, fluorescence emission, and Fourier transform-infrared spectroscopy indicate an unstructured conformation for the nematode protein. Therefore, in solution, no evidence was found to support structure predictions; instead, AavLEA1 seems to be natively unfolded with a high degree of hydration and low compactness. Such proteins can, however, be induced to fold into more rigid structures by partner molecules or by altered physiological conditions. Because AavLEA1 is associated with desiccation stress, its Fourier transform-infrared spectrum in the dehydrated state was examined. A dramatic but reversible increase in alpha -helix and, possibly, coiled coil formation was observed on drying, indicating that computer predictions of secondary structure may be correct for the solid state. This unusual finding offers the possibility that structural shifts in Group 3 LEA proteins occur on dehydration, perhaps consistent with their role in anhydrobiosis.

* This work was funded by grants from the Leverhulme Trust, the Isaac Newton Trust, the Royal Irish Academy, and the Royal Society.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ A Science Foundation Ireland Investigator. Present address: Domantis Limited, Granta Park, Cambridge CB1 6GS, UK.

** The AWG Senior Research Fellow of Pembroke College, Cambridge. To whom correspondence should be addressed: Institute of Biotechnology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QT, UK. Tel.: 44-1223-766549; Fax: 44-1223-334162; E-mail: at10004@biotech.cam.ac.uk.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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