C. elegans HIM-8 functions outside of meiosis to antagonize EGL-13 Sox protein function.

Nelms BL, Hanna-Rose W
Dev Biol. 2006 293 (2): 392-402

PMID: 16546157 · DOI:10.1016/j.ydbio.2006.02.010

egl-13 encodes a Sox domain protein that is required for proper uterine seam cell development in Caenorhabditis elegans. We demonstrate that mutations of the C2H2 zinc fingers encoded by the him-8 (high incidence of males) gene partially suppress the egg-laying and connection-of-gonad morphology defects caused by incompletely penetrant alleles of egl-13. him-8 alleles have previously characterized recessive effects on recombination and segregation of the X chromosome during meiosis due to failure of X chromosome homolog pairing and subsequent synapsis. However, we show that him-8 alleles are semi-dominant suppressors of egl-13, and the semi-dominant effect is due to haplo-insufficiency of the him-8 locus. Thus, we conclude that the wild-type him-8 gene product acts antagonistically to EGL-13. Null alleles of egl-13 cannot be suppressed, suggesting that this antagonistic interaction most likely occurs either upstream of or in parallel with EGL-13. Moreover, we conclude that suppression of egl-13 is due to a meiosis-independent function of him-8 because suppression is observed in mutants that have severely reduced meiotic germ cell populations and suppression does not depend on the function of him-8 in the maternal germ line. We also show that the chromosomal context of egl-13 seems important in the him-8 suppression mechanism. Interactions between these genes can give insight into function of Sox family members, which are important in many aspects of metazoan development, and into functions of him-8 outside of meiosis.

MeSH Terms (18)

Alleles Animals Animals, Genetically Modified Base Sequence Caenorhabditis elegans Caenorhabditis elegans Proteins Cell Cycle Proteins DNA, Helminth Female Genes, Helminth Male Meiosis Mutation RNA Interference Suppression, Genetic Transcription Factors Uterus Vulva

Connections (1)

This publication is referenced by other Labnodes entities: