Conservation of the Caenorhabditis elegans cuticle collagen gene col-12 in Caenorhabditis briggsae

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• 作者：Gilleard ; John S. ; Henderson ; Douglas K. ; Ulla ; Noreen
• 关键词：Exoskeleton ; Extracellular matrix ; Nematode ; Phylogenetic comparison ; aa ; amino acid(s) ; bp ; base pair(s) ; dpy ; dumpy ; E ; EcoRI restriction site ; Gly ; glycine ; kb ; kilobase(s) or 1000 bp ; kDa ; kilodalton(s) ; nt ; nucleotide(s) ; PCR ; polymerase chain reacti
• 刊名：Gene
• 出版年：1997
• 出版时间：July 9, 1997
• 年：1997
• 卷：193
• 期：2
• 页码：181-186
• 全文大小：579 K

文摘

The functional importance of the majority of Caenorhabditis elegans cuticle collagen genes is unknown. We have identified, cloned and sequenced the Caenorhabditis briggsae homologue of the C. elegans gene col-12, a cuticle collagen for which no mutants have yet been identified. Homology in the flanking sequence has allowed us to unambiguously identify this gene as the col-12 homologue, as opposed to some other closely related member of this large multigene family. The whole of the predicted polypeptide is highly conserved (94.9 % identical), including those regions not yet shown by mutational analysis to be important for C. elegans cuticle collagen function. These include the whole of the N-terminal non-Gly-X-Y domain and the X and Y positions of the Gly-X-Y domain. This may be a consequence of the requirement of cuticle collagens to participate in intermolecular interactions throughout the full length of the polypeptide. There is increasing evidence to suggest that conservation between C. elegans and C. briggsae is confined to functionally significant sequence. Hence, the conservation of col-12 between these two species provides evidence that this member of the cuticle collagen family has a significant structural function.