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. 2018 Oct 11;9:4206. doi: 10.1038/s41467-018-06185-2

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — The cysteine-based code for collagen C-Pro assembly is generalizable across the fibrillar collagens. a Alignment of the interstrand disulfide-bonding region of the human fibrillar collagen C-propeptides highlights that C-Pro domains known to homotrimerize contain all four conserved cysteine residues, whereas C-Pro domains known to only form heterotrimers lack a single cysteine at C2 or C3. The residue colored red in each protein sequence corresponds to the mutated residue analyzed in b, c. Amino acid numbering was derived from the corresponding full-length procollagens. b Immunoblot analyses of individually expressed wild-type fibrillar collagen C-Pro domains known to only form heterotrimers. Assembly was analyzed under non-reducing and reducing conditions. Wild-type variants (HA-tagged; red) all migrated as monomers, while all variants in which the missing cysteine residue was re-introduced (FLAG-tagged; green) gained the ability to homotrimerize in a disulfide-dependent manner. c Immunoblot analysis of individually expressed wild-type fibrillar collagen C-Pro domains known to have the capacity to homotrimerize. Assembly was analyzed under non-reducing and reducing conditions. Wild-type variants (HA-tagged; red) all migrated as disulfide-dependent homotrimers, while variants in which a single cysteine residue was mutated to serine (FLAG-tagged; green) lost the capacity to form disulfide-linked homotrimers. Note that C-Proα2(XI) was not secreted and was detected only in cell lysate. d Co-expression of the wild-type C-Proα1(III) domain with the C2S C-Proα1(III) demonstrates the wild-type protein’s ability to rescue the monomeric C2S variant into a disulfide-linked trimer, shown by the overlap of green and red signal (yellow)