The role of coiled-coil α-Helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits: A mutational analysis

Dominik R Haudenschild, M. Mehrdad Tondravi, Urs Hofer, Qian Chen, Paul F. Goetinck

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Cartilage matrix protein (CMP) exists as a disulfide-bonded homotrimer in the matrix of cartilage. Each monomer consists of two CMP-A domains that are separated by an epidermal growth factor-like domain. A heptad repeat-containing tail makes up the carboxyl-terminal domain of the protein. The secreted form of CMP contains 12 cysteine residues numbered C1 through C12. Two of these are in each of the CMP-A domains, six are in the epidermal growth factor-like domain, and two are in the heptad repeat-containing tail. Two major categories of mutant CMPs were generated to analyze the oligomerization process of CMP: a mini-CMP and a heptadless full-length CMP. The mini-CMP consists of the CMP-A2 domain and the heptad repeat-containing tail. In addition, a number of mutations affecting C9 through C12 were generated within the full-length, the mini-, and the heptad-less CMPs. The mutational analysis indicates that the heptad repeats are necessary for the initiation of CMP trimerization and that the two cysteines in the heptad repeat-containing tail are both necessary and sufficient to form intermolecular disulfide bonds in either full-length or mini-CMP. The two cysteines within a CMP-A domain form an intradomain disulfide bond.

Original languageEnglish (US)
Pages (from-to)23150-23154
Number of pages5
JournalJournal of Biological Chemistry
Volume270
Issue number39
StatePublished - Sep 29 1995
Externally publishedYes

Fingerprint

Matrilin Proteins
Protein Subunits
Disulfides
Stabilization
Staphylococcal Protein A
Cytidine Monophosphate
Cysteine
Epidermal Growth Factor
Protein Multimerization
Oligomerization
Cartilage
varespladib methyl

ASJC Scopus subject areas

  • Biochemistry

Cite this

The role of coiled-coil α-Helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits : A mutational analysis. / Haudenschild, Dominik R; Tondravi, M. Mehrdad; Hofer, Urs; Chen, Qian; Goetinck, Paul F.

In: Journal of Biological Chemistry, Vol. 270, No. 39, 29.09.1995, p. 23150-23154.

Research output: Contribution to journalArticle

@article{a640c5bf47134b65b690cce87a8736c5,
title = "The role of coiled-coil α-Helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits: A mutational analysis",
abstract = "Cartilage matrix protein (CMP) exists as a disulfide-bonded homotrimer in the matrix of cartilage. Each monomer consists of two CMP-A domains that are separated by an epidermal growth factor-like domain. A heptad repeat-containing tail makes up the carboxyl-terminal domain of the protein. The secreted form of CMP contains 12 cysteine residues numbered C1 through C12. Two of these are in each of the CMP-A domains, six are in the epidermal growth factor-like domain, and two are in the heptad repeat-containing tail. Two major categories of mutant CMPs were generated to analyze the oligomerization process of CMP: a mini-CMP and a heptadless full-length CMP. The mini-CMP consists of the CMP-A2 domain and the heptad repeat-containing tail. In addition, a number of mutations affecting C9 through C12 were generated within the full-length, the mini-, and the heptad-less CMPs. The mutational analysis indicates that the heptad repeats are necessary for the initiation of CMP trimerization and that the two cysteines in the heptad repeat-containing tail are both necessary and sufficient to form intermolecular disulfide bonds in either full-length or mini-CMP. The two cysteines within a CMP-A domain form an intradomain disulfide bond.",
author = "Haudenschild, {Dominik R} and Tondravi, {M. Mehrdad} and Urs Hofer and Qian Chen and Goetinck, {Paul F.}",
year = "1995",
month = "9",
day = "29",
language = "English (US)",
volume = "270",
pages = "23150--23154",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "39",

}

TY - JOUR

T1 - The role of coiled-coil α-Helices and disulfide bonds in the assembly and stabilization of cartilage matrix protein subunits

T2 - A mutational analysis

AU - Haudenschild, Dominik R

AU - Tondravi, M. Mehrdad

AU - Hofer, Urs

AU - Chen, Qian

AU - Goetinck, Paul F.

PY - 1995/9/29

Y1 - 1995/9/29

N2 - Cartilage matrix protein (CMP) exists as a disulfide-bonded homotrimer in the matrix of cartilage. Each monomer consists of two CMP-A domains that are separated by an epidermal growth factor-like domain. A heptad repeat-containing tail makes up the carboxyl-terminal domain of the protein. The secreted form of CMP contains 12 cysteine residues numbered C1 through C12. Two of these are in each of the CMP-A domains, six are in the epidermal growth factor-like domain, and two are in the heptad repeat-containing tail. Two major categories of mutant CMPs were generated to analyze the oligomerization process of CMP: a mini-CMP and a heptadless full-length CMP. The mini-CMP consists of the CMP-A2 domain and the heptad repeat-containing tail. In addition, a number of mutations affecting C9 through C12 were generated within the full-length, the mini-, and the heptad-less CMPs. The mutational analysis indicates that the heptad repeats are necessary for the initiation of CMP trimerization and that the two cysteines in the heptad repeat-containing tail are both necessary and sufficient to form intermolecular disulfide bonds in either full-length or mini-CMP. The two cysteines within a CMP-A domain form an intradomain disulfide bond.

AB - Cartilage matrix protein (CMP) exists as a disulfide-bonded homotrimer in the matrix of cartilage. Each monomer consists of two CMP-A domains that are separated by an epidermal growth factor-like domain. A heptad repeat-containing tail makes up the carboxyl-terminal domain of the protein. The secreted form of CMP contains 12 cysteine residues numbered C1 through C12. Two of these are in each of the CMP-A domains, six are in the epidermal growth factor-like domain, and two are in the heptad repeat-containing tail. Two major categories of mutant CMPs were generated to analyze the oligomerization process of CMP: a mini-CMP and a heptadless full-length CMP. The mini-CMP consists of the CMP-A2 domain and the heptad repeat-containing tail. In addition, a number of mutations affecting C9 through C12 were generated within the full-length, the mini-, and the heptad-less CMPs. The mutational analysis indicates that the heptad repeats are necessary for the initiation of CMP trimerization and that the two cysteines in the heptad repeat-containing tail are both necessary and sufficient to form intermolecular disulfide bonds in either full-length or mini-CMP. The two cysteines within a CMP-A domain form an intradomain disulfide bond.

UR - http://www.scopus.com/inward/record.url?scp=0028981360&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028981360&partnerID=8YFLogxK

M3 - Article

C2 - 7559460

AN - SCOPUS:0028981360

VL - 270

SP - 23150

EP - 23154

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 39

ER -