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Originally published In Press as doi:10.1074/jbc.M206278200 on December 26, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8065-8074, March 7, 2003
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The FAR Protein Family of the Nematode Caenorhabditis elegans
DIFFERENTIAL LIPID BINDING PROPERTIES, STRUCTURAL CHARACTERISTICS, AND DEVELOPMENTAL REGULATION*

Antonio Garofaloa, Marie-Claire Rowlinsona, Ngwa A. Amambuaa, Jacqueline M. Hughesb, Sharon M. Kellyc, Nicholas C. Pricec, Alan Cooperd, David G. Watsone, Malcolm W. Kennedyfgh, and Janette E. Bradleyagi

From the a School of Life and Environmental Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, Great Britain, the b Department of Biological Sciences, Salford University, Salford M5 4WT, Great Britain, the c Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, and the d Department of Chemistry, Joseph Black Bldg., University of Glasgow, Glasgow G12 8QQ, Scotland, the e Department of Pharmaceutical Sciences, University of Strathclyde, Glasgow G4 0NR, Scotland, and the f Division of Environmental and Evolutionary Biology, Institute of Biomedical and Life Sciences, Graham Kerr Bldg., University of Glasgow, Glasgow G12 8QQ, Scotland, Great Britain

Parasitic nematodes of humans and plants secrete a structurally novel type of fatty acid- and retinol-binding protein, FAR, into the tissues they occupy. These proteins may interfere with intercellular lipid signaling to manipulate the defense reactions of the host or acquire essential lipids for the parasites. The genome of the nematode Caenorhabditis elegans encodes eight FAR-like proteins (Ce-FAR-1 to -8). These fall into three discrete groups as indicated by phylogenetic sequence comparisons and intron positions, the proteins from parasitic nematodes falling into group A. Recombinant Ce-FAR-1 to -7 were produced in Escherichia coli and tested for lipid binding in fluorescence-based assays. Ce-FAR-1 to -6 bound DAUDA (11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid), cis-parinaric acid, and retinol with dissociation constants in the micromolar range, whereas Ce-FAR-7 bound the latter two lipids relatively poorly. Each protein produced a characteristic shift in peak fluorescence emission of DAUDA, and one (Ce-FAR-5) produced a shift greater than has been observed previously for any lipid-binding protein. Selected Ce-FAR proteins were analyzed by circular dichroism (CD) and differential scanning calorimetry, were found to be helix-rich, and exhibited high thermal stability (transition midpoint, 82.7 °C). CD and secondary structure predictions, however, both indicated that Ce-FAR-7 possesses substantially less helix than the other FAR proteins. The genes encoding the Ce-FAR proteins were found to be transcribed differentially through the life cycle of C. elegans, such that Ce-far-4 was transcribed at highest levels in the fourth larval stage, and Ce-far-3 and -7 predominated in males.

* This work was supported by grants from the Universities of Salford and Nottingham (to J. E. B.) and the Wellcome Trust (to M. W. K.). The circular dichroism and biological calorimetry facilities were supported by the University of Glasgow and the Biotechnology and Biological Sciences Research Council (UK), the fluorometry facilities were supported by the University of Glasgow, and the GC-MS instrument was provided by a Wellcome Trust grant (to D. G. W. and M. W. K.).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.

g Both authors contributed equally to this work.

h To whom correspondence should be addressed. Tel.: 44-141-330-5819; Fax: 44-141-330-5971; E-mail: malcolm.kennedy@bio.gla.ac.uk.

i To whom correspondence should be addressed. Tel.: 44-115-951-3207; Fax: 44-150-951-3251; E-mail: jan.bradley@nottingham.ac.uk.

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