Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm.

PloS One
Elena Makareeva, Sergey Leikin

Abstract

Fibers composed of type I collagen triple helices form the organic scaffold of bone and many other tissues, yet the energetically preferred conformation of type I collagen at body temperature is a random coil. In fibers, the triple helix is stabilized by neighbors, but how does it fold? The observations reported here reveal surprising features that may represent a new paradigm for folding of marginally stable proteins. We find that human procollagen triple helix spontaneously folds into its native conformation at 30-34 degrees C but not at higher temperatures, even in an environment emulating Endoplasmic Reticulum (ER). ER-like molecular crowding by nonspecific proteins does not affect triple helix folding or aggregation of unfolded chains. Common ER chaperones may prevent aggregation and misfolding of procollagen C-propeptide in their traditional role of binding unfolded polypeptide chains. However, such binding only further destabilizes the triple helix. We argue that folding of the triple helix requires stabilization by preferential binding of chaperones to its folded, native conformation. Based on the triple helix folding temperature measured here and published binding constants, we deduce that HSP47 is likely to do just th...Continue Reading

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Citations

Jan 13, 2009·Journal of Lipid Research·Mark H DoolittleHoward Wong
May 8, 2009·The Journal of Biological Chemistry·Yoshihiro IshikawaHans Peter Bächinger
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Apr 2, 2020·BMC Molecular and Cell Biology·Essak S KhanAránzazu Del Campo
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Methods Mentioned

BETA
electrophoresis
circular dichroism
glycosylation
ion exchange chromatography
Scanning Circular Dichroism

Software Mentioned

Osteogenesis Imperfecta

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