TAILIEUCHUNG - Báo cáo khoa học: The astacin protein family in Caenorhabditis elegans

In the nematodeCaenorhabditis elegans, 40 genes code for astacin-likeproteins (nematodeastacins,NAS).The astacins are metalloproteases present in bacteria, invertebrates and vertebrates and serve avarietyof physiological functions like digestion, hatching, peptide processing, morphogenesis and pattern formation. With the exception of one distorted pseudogene, all the otherC. elegansastacins are expressed and are evidently functional. For 13 genes we found splicing patterns differing from the Genefinder predictions in WormBase, sometimes markedly | Eur. J. Biochem. 270 4909-4920 2003 FEBS 2003 doi The astacin protein family in Caenorhabditis elegans Frank Mohrlen1 Harald Hutter2 and Robert Zwilling1 Institute of Zoology University of Heidelberg 2Max-Planck-Institute for Medical Research Heidelberg Germany In the nematode Caenorhabditis elegans 40 genes code for astacin-like proteins nematode astacins NAS . The astacins are metalloproteases present in bacteria invertebrates and vertebrates and serve a variety of physiological functions like digestion hatching peptide processing morphogenesis and pattern formation. With the exception of one distorted pseudogene all the other C. elegans astacins are expressed and are evidently functional. For 13 genes we found splicing patterns differing from the Genefinder predictions in WormBase sometimes markedly. The GFP expression pattern for NAS-4 shows a specific localization in anterior pharynx cells and in the whole digestive tract as the secreted form . In contrast NAS-7 is found in the head of adult hermaphrodites but not in pharynx cells or in the lumen of the digestive tract. In embryos NAS-7 fluorescence becomes detectable just before hatching. In C. elegans astacins three basic structural and functional moieties can be discerned a prepro portion the central catalytic chain and long C-terminal extensions with presumably regulatory functions. Within the regulatory moiety EFG-like CUB SXC and TSP-1 domains can be distinguished. Based on structural differences of the regulatory unit we established six NAS subgroups which seemingly represented different functional and evolutionary clusters. This pattern deduced exclusively from the domain arrangement in the regulatory moiety is perfectly reflected in an evolutionary tree constructed solely from amino acid sequence information of the catalytic chain. Related catalytic chains tend to have related regulatory extensions. The notable gene NAS-39 shows a striking resemblance to human BMP-1 .

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