Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparan sulfate proteoglycan

Genes Dev. 1993 Aug;7(8):1471-84. doi: 10.1101/gad.7.8.1471.

Abstract

Mutations in the unc-52 gene of Caenorhabditis elegans affect attachment of the myofilament lattice to the muscle cell membrane. Here, we demonstrate that the unc-52 gene encodes a nematode homolog of perlecan, the mammalian basement membrane heparan sulfate proteoglycan. The longest potential open reading frame of this gene encodes a 2482-amino-acid protein with a signal peptide and four domains. The first domain is unique to the unc-52 polypeptide, whereas the three remaining domains contain sequences found in the LDL receptor (domain II) laminin (domain III) and N-CAM (domain IV). We have identified three alternatively spliced transcripts that encode different carboxy-terminal sequences. The two larger transcripts encode proteins containing all or part of domain IV, whereas the smaller transcript encodes a shortened polypeptide that completely lacks domain IV. We have determined that the disorganized muscle phenotype observed in unc-52(st196) animals is caused by the insertion of a Tc1 transposon into domain IV. Two monoclonal antibodies that recognize an extracellular component of all contractile tissues in C. elegans fail to stain embryos homozygous for a lethal unc-52 allele. We have mapped the epitopes recognized by both monoclonal antibodies to a region of domain IV in the unc-52-encoded protein sequence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / chemistry
  • Amino Acid Sequence
  • Animals
  • Basement Membrane / chemistry*
  • Caenorhabditis elegans / genetics*
  • Caenorhabditis elegans Proteins*
  • Cell Adhesion Molecules, Neuronal / chemistry
  • Cloning, Molecular
  • Conserved Sequence
  • DNA Transposable Elements
  • Genes, Helminth*
  • Helminth Proteins / chemistry*
  • Helminth Proteins / genetics
  • Heparan Sulfate Proteoglycans*
  • Heparitin Sulfate / chemistry*
  • Heparitin Sulfate / genetics
  • Immunoglobulins / chemistry
  • Immunoglobulins / genetics
  • Laminin / chemistry
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Muscle Contraction / genetics
  • Muscle Proteins / chemistry*
  • Mutagenesis, Insertional
  • Open Reading Frames
  • Proteoglycans / chemistry*
  • Proteoglycans / genetics
  • Receptors, LDL / chemistry
  • Recombinant Fusion Proteins / chemistry
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Caenorhabditis elegans Proteins
  • Cell Adhesion Molecules, Neuronal
  • DNA Transposable Elements
  • Helminth Proteins
  • Heparan Sulfate Proteoglycans
  • Immunoglobulins
  • Laminin
  • Membrane Proteins
  • Muscle Proteins
  • Proteoglycans
  • Receptors, LDL
  • Recombinant Fusion Proteins
  • unc-52 protein, C elegans
  • perlecan
  • Heparitin Sulfate

Associated data

  • GENBANK/L11593
  • GENBANK/L11594
  • GENBANK/L13458
  • GENBANK/L15616
  • GENBANK/L16016
  • GENBANK/L24529
  • GENBANK/S56762
  • GENBANK/S56763
  • GENBANK/Z15047
  • GENBANK/Z15048