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Volume 271, Number 46, Issue of November 15, 1996 pp. 29003-29008
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Involvement of Prolyl 4-Hydroxylase in the Assembly of Trimeric Minicollagen XII
STUDY IN A BACULOVIRUS EXPRESSION SYSTEM

(Received for publication, April 17, 1996, and in revised form, July 18, 1996)

Marlène Mazzorana Dagger , Anne Snellman , Kari I. Kivirikko , Michel van der Rest Dagger and Taina Pihlajaniemi

From the Dagger  Institut de Biologie et Chimie des Protéines, IBCP CNRS UPR 412, 7, Passage du Vercors, 69367 Lyon Cedex 07, France and the  Collagen Research Unit, Biocenter and Department of Medical Biochemistry, University of Oulu, FIN-90220 Oulu, Finland

We have shown previously that hydroxylation played a critical role in the trimer assembly and disulfide bonding of the three constituent alpha  chains of a minicollagen composed of the extreme C-terminal collagenous (COL1) and noncollagenous (NC1) domains of type XII collagen in HeLa cells (Mazzorana, M., Gruffat, H., Sergeant, A., and van der Rest, M. (1993) J. Biol. Chem. 268, 3029-3032). We have further characterized the involvement of prolyl 4-hydroxylase in the assembly of the three alpha  chains to form trimeric disulfide-bonded type XII minicollagen in an insect cell expression system. For this purpose, type XII minicollagen was produced in insect cells from baculovirus vectors, alone or together with wild-type human prolyl 4-hydroxylase or with the human enzyme mutated in the catalytic site of its alpha  or beta  subunits or with the individual alpha  or beta  subunits. When type XII minicollagen was produced alone, negligible amounts of disulfide-bonded trimers were found to be produced by the cells. However, coproduction of the collagen with the two subunits of the wild-type human enzyme dramatically increased the amount of disulfide-bonded trimeric type XII minicollagen molecules. In contrast, coproduction of the collagen with alpha  subunits that had a mutation completely inactivating the human enzyme failed to enhance the trimer assembly. These results directly show that an active prolyl 4-hydroxylase is required for the assembly of disulfide-bonded trimers of type XII minicollagen.


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