Abstract

GLD‐1 is a prototypical member of the STAR class of proteins, which are highly conserved among higher eukaryotes and seem to play a general role in posttranscriptional gene regulation. In the C. elegans hermaphrodite germ line, GLD‐1 is essential for inducing meiosis. Furthermore, it triggers the spermatogenesis‐to‐oogenesis switch by regulating the differentiation of germ line stem cells. GLD‐1 translationally represses the expression of proteins promoting oogenesis by binding to the 3′ untranslated region of their messenger RNAs (mRNAs). GLD‐1 homodimers recognize 28 nucleotide repeats within the mRNA. Each repeat can accommodate one GLD‐1 dimer.Even though the structures of a few homologous STAR protein RNA binding subdomains have been determined, no structural information is available on the homodimerization subdomain. Our structural characterization of the GLD‐1 homodimerization domain by CD, NMR and EPR spectroscopy points towards a α‐helical, antiparallel coiled‐coil dimeric structure.

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