Authors: Munier AI; Medzhitov R; Janeway CA Jr; Doucet D; Capovilla M; Lagueux M
Abstract: Serine proteases play vital roles in several biological processes such as development and immunity. We have characterized Graal, a large multi-domain serine protease from Drosophila. Graal is spliced in at least three transcripts that are present throughout development. The domains found in Graal proteins are: chitin-binding domains (CBD), scavenger receptor cysteine-rich (SRCR) domains, low density lipoprotein receptor cysteine-rich (LDLR-CR) domains, histidine and proline-rich domains, a NGGYQPP-repeat domain and a serine protease domain. The last 2370 nucleotides of these RNAs are identical and encode a His-rich domain, two SRCR domains, two LDLR-CR domains and a protease domain. The transcription of graal is upregulated after fungal or bacterial infection. Analysis of the Iso1 (y;cn,sp,bw) strain shows that graal transcription is impaired in this fly line due to the insertion of a retrotransposon in the sixth exon. However, no phenotype could be observed consecutive to the absence of graal full length transcripts, particularly in the context of an immune challenge.Keywords: Amino Acid Sequence; Animals; Animals, Genetically Modified; Base Sequence; Cloning, Molecular; DNA, Complementary/genetics; Drosophila/*enzymology/*genetics/immunology; *Genes, Insect; Isoenzymes/chemistry/genetics/physiology; Molecular Sequence Data; Protein Structure, Tertiary; RNA, Messenger/genetics/metabolism; Sequence Homology, Amino Acid; Serine Endopeptidases/chemistry/*genetics/physiology
Journal: Insect biochemistry and molecular biology
Date: Oct. 12, 2004
Select reference article to upload
Munier AI, Medzhitov R, Janeway CA Jr, Doucet D, Capovilla M, Lagueux M (2004) graal: a Drosophila gene coding for several mosaic serine proteases. Insect biochemistry and molecular biology 34: 1025-35.