Mutagenesis of the cysteine-rich clip domain in the Drosophila patterning protease, Snake.

ABSTRACT: A common motif found in invertebrate serine proteases involved in immunity and development is the clip domain, proposed to regulate catalytic activity or protein-protein interactions within proteolytic cascades. Snake functions in a cascade that patterns the Drosophila embryo, and provides an accessible model for exploring the structural requirements for clip domain function. We tested Snake zymogens bearing charged-to-alanine mutations in the clip domain for their ability to rescue embryos lacking endogenous Snake and for their interactions by S2 cell co-transfection with upstream Gastrulation Defective and downstream Easter in the protease cascade. Of 13 single and multiple substitutions, one double mutant in a predicted protruding region exhibited a severe defect in embryonic rescue but

SUBMITTER: Tian S 

PROVIDER: S-EPMC2518291 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature