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Volume 271, Number 35, Issue of August 30, 1996 pp. 21566-21573
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Triple Helix Formation of Procollagen Type I Can Occur at the Rough Endoplasmic Reticulum Membrane

(Received for publication, February 7, 1996, and in revised form, April 15, 1996)

Konrad Beck , Bruce A. Boswell , Catherine C. Ridgway and Hans Peter Bächinger ^¶

From the  Shriners Hospital for Children, Research Unit, Portland, Oregon 97201 and the ^¶ Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201

One key problem in understanding the biosynthesis of collagens remains the assembly of the three -chains. How and when are the different gene products selected, aligned, and folded into a triple helix? As the spatial arrangement during biosynthesis might be important, we concentrated on whether the rough endoplasmic reticular membrane is involved in this process. Microsomes were prepared from biosynthetically labeled chick tendon fibroblasts. Vesicles were spread as a monomolecular film which was then transferred over several compartments of a filmbalance containing fresh subphase. Fluorograms of the surface film showed that the monolayer contains procollagen chains. When the monolayer was transferred onto a chymotrypsin/trypsin-containing subphase, the gel bands of the pro-chains were shifted into the position of mature -chains, indicating that only the propeptides were digested and the collagenous regions were protected due to triple helix formation. Our results suggest that newly synthesized pro-chains can associate as trimers and fold into a triple helical conformation while they are still associated with the membranes of the rough endoplasmic reticulum. These processes also occur when interchain disulfide linkage is inhibited, indicating that chain selection and registration is not dependent on formation of covalent bonds among the carboxyl propeptides.

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