Reference - Detail
| RRC ID | 4457 |
|---|---|
| Author | Thein MC, Winter AD, Stepek G, McCormack G, Stapleton G, Johnstone IL, Page AP. |
| Title | Combined extracellular matrix cross-linking activity of the peroxidase MLT-7 and the dual oxidase BLI-3 is critical for post-embryonic viability in Caenorhabditis elegans. |
| Journal | J Biol Chem |
| Abstract |
The nematode cuticle is a protective collagenous extracellular matrix that is modified, cross-linked, and processed by a number of key enzymes. This Ecdysozoan-specific structure is synthesized repeatedly and allows growth and development in a linked degradative and biosynthetic process known as molting. A targeted RNA interference screen using a cuticle collagen marker has been employed to identify components of the cuticle biosynthetic pathway. We have characterized an essential peroxidase, MoLT-7 (MLT-7), that is responsible for proper cuticle molting and re-synthesis. MLT-7 is an active, inhibitable peroxidase that is expressed in the cuticle-synthesizing hypodermis coincident with each larval molt. mlt-7 mutants show a range of body morphology defects, most notably molt, dumpy, and early larval stage arrest phenotypes that can all be complemented with a wild type copy of mlt-7. The cuticles of these mutants lacks di-tyrosine cross-links, becomes permeable to dye and accessible to tyrosine iodination, and have aberrant collagen protein expression patterns. Overexpression of MLT-7 causes mutant phenotypes further supporting its proposed enzymatic role. In combination with BLI-3, an H2O2-generating NADPH dual oxidase, MLT-7 is essential for post-embryonic development. Disruption of mlt-7, and particularly bli-3, via RNA interference also causes dramatic changes to the in vivo cross-linking patterns of the cuticle collagens DPY-13 and COL-12. This points toward a functionally cooperative relationship for these two hypodermally expressed proteins that is essential for collagen cross-linking and proper extracellular matrix formation. |
| Volume | 284(26) |
| Pages | 17549-63 |
| Published | 2009-6-26 |
| DOI | 10.1074/jbc.M900831200 |
| PII | S0021-9258(19)82038-0 |
| PMID | 19406744 |
| PMC | PMC2719394 |
| MeSH | Amino Acid Sequence Animals Animals, Genetically Modified Caenorhabditis elegans / embryology* Caenorhabditis elegans Proteins / metabolism* Collagen / metabolism* Cross-Linking Reagents / metabolism Embryo, Nonmammalian / metabolism* Extracellular Matrix / metabolism* Female Gene Expression Regulation, Developmental Male Molecular Sequence Data Mutation / genetics NADPH Oxidases / metabolism* Peroxidases / metabolism* Phenotype RNA Interference Recombinant Proteins / genetics Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism Sequence Homology, Amino Acid |
| IF | 4.238 |
| Times Cited | 55 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
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| Total number of mentions | 0 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| C.elegans | tm1794 |