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Originally published In Press as doi:10.1074/jbc.M201865200 on April 25, 2002

J. Biol. Chem., Vol. 277, Issue 26, 23965-23971, June 28, 2002
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Cloning and Characterization of a Low Molecular Weight Prolyl 4-Hydroxylase from Arabidopsis thaliana
EFFECTIVE HYDROXYLATION OF PROLINE-RICH, COLLAGEN-LIKE, AND HYPOXIA-INDUCIBLE TRANSCRIPTION FACTOR alpha -LIKE PEPTIDES*

Reija Hieta and Johanna MyllyharjuDagger

From the Collagen Research Unit, Biocenter Oulu and the Department of Medical Biochemistry and Molecular Biology, University of Oulu, FIN-90014 Oulu, Finland

4-Hydroxyproline is found in collagens and collagen-like proteins in animals and in many glycoproteins in plants. Animal prolyl 4-hydroxylases (P4Hs) have been cloned and characterized from many sources, but no plant P4H has been cloned so far. We report here that the genome of Arabidopsis thaliana encodes six P4H-like polypeptides, one of which, a 283-residue soluble monomer, was cloned and characterized here as a recombinant protein. Catalytically critical residues identified in animal P4Hs are conserved in this P4H, and their mutagenesis led to complete or almost complete inactivation. The recombinant P4H effectively hydroxylated poly(L-proline) and many synthetic peptides corresponding to proline-rich repeats present in plant glycoproteins and other proteins. Surprisingly, collagen-like peptides were also good substrates, the Vmax with (Pro-Pro-Gly)10 being similar to that with poly(L-proline). The enzyme acted in this peptide preferentially on prolines in Y positions in the X-Y-Gly triplets. Correspondingly, (Gly-Pro-4Hyp)5 and (Pro-Ala-Gly)5 were poor substrates, with Vmax values less than 5 and 20% of that obtained with (Pro-Pro-Gly)10, respectively, the Km for the latter also being high. Peptides representing the N- and C-terminal hydroxylation sites present in hypoxia-inducible transcription factor alpha  also served as substrates. As these peptides contain only one proline residue, a poly(L-proline) type II conformation was clearly not required for hydroxylation.

* This work was supported by a Health Science Council grant and by Grant 44843 from the Finnish Centre of Excellence Programme 2000-2005 of the Academy of Finland.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.

Dagger To whom correspondence should be addressed: Dept. of Medical Biochemistry and Molecular Biology, P. O. Box 5000, University of Oulu, FIN-90014 Oulu, Finland. Tel.: 358-8-537-5740; Fax: 358-8-537-5811; E-mail: johanna.myllyharju@oulu.fi.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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