ArticleGenetics1994
Mutational analysis of the Drosophila snake protease: an essential role for domains within the proenzyme polypeptide chain.
Article in Genetics, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 45 citations in OpenAlex.
- Comparative Transcriptome Analysis ofInsects · 2019Article
- Pipe-dependent ventral processing of Easter by Snake is the defining step in Drosophila embryo DV axis formation.Current biology : CB · 2010Article
- Mutagenesis of the cysteine-rich clip domain in the Drosophila patterning protease, Snake.Archives of biochemistry and biophysics · 2008Article
- Mutational analysis of Stubble-stubbloid gene structure and function in Drosophila leg and bristle morphogenesis.Genetics · 2006Article
- Gastrulation defective, a complement factor C2/B-like protease, interprets a ventral prepattern in Drosophila.EMBO reports · 2001Article
- Autoproteolysis and feedback in a protease cascade directing Drosophila dorsal-ventral cell fate.The EMBO journal · 2001Article
- Gastrulation defective is a serine protease involved in activating the receptor toll to polarize the Drosophila embryo.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- The gastrulation defective gene of Drosophila melanogaster is a member of the serine protease superfamily.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Evolutionary conservation and predicted structure of the Drosophila extra sex combs repressor protein.Molecular and cellular biology · 1997Article
- Complete sequence of the bithorax complex of Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes involved in the generation of dorsoventral asymmetry in the developing Drosophila melanogaster embryo, snake and easter, encode the zymogen form of serine proteases. Mutant alleles of snake were cloned and sequenced revealing two types of lesions: point mutations which alter the amino acid sequence (snk073 and snkrm4) and point mutations which alter the splicing (snk229 or snk233) of intron 1 of the mRNA from the normal 3' end of the intron to a cryptic site. snake mutant embryos derived from homozygous mothers can be fully rescued by injection of RNA transcripts of the wild-type snake cDNA. RNA phenotypic rescue and site-directed mutagenesis experiments indicate that snake requires the serine, histidine and aspartic acid of the catalytic triad for normal activity. Deletion experiments show that an acidic proenzyme domain is required for snake rescue activity to be uniformly distributed throughout the embryo. A second proenzyme domain, called the disulfide knot, appears to be essential for normal regulation of activity of the snake catalytic chain. Transcripts encoding only the proenzyme polypeptides of either snake or easter can dorsalize wild type embryos. We propose a model in which the proenzyme determinants of both the snake and easter enzymes mediate interaction between the serine proteases and other components of the dorsal-ventral patterning system.
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