Fertilization in C. elegans requires an intact C-terminal RING finger in sperm protein SPE-42.

ABSTRACT:

Background

The C. elegans sperm protein SPE-42, a membrane protein of unknown structure and molecular function, is required for fertilization. Sperm from worms with spe-42 mutations appear normal but are unable to fertilize eggs. Sequence analysis revealed the presence of 8 conserved cysteine residues in the C-terminal cytoplasmic domain of this protein suggesting these residues form a zinc-coordinating RING finger structure.

Results

We made an in silico structural model of the SPE-42 RING finger domain based on primary sequence analysis and previously reported RING structures. To test the model, we created spe-42 transgenes coding for mutations in each of the 8 cysteine residues predicted to coordinate Zn++ ions in the RING finger motif. Transgenes were crossed into a spe-4

SUBMITTER: Wilson LD 

PROVIDER: S-EPMC3053230 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature