FOG-2, a novel F-box containing protien, associates with the GLD-1 RNA binding protein and directs male sex determination in the C. elegans hermaphrodite germline

R. Clifford, M. H. Lee, S. Nayak, M. Ohmachi, F. Giorgini, T. Schedl

Research output: Contribution to journalArticlepeer-review

123 Scopus citations

Abstract

Male sex determination in the Caenorhabditis elegans hermaphrodite germline requires translational repression of tra-2 mRNA by the GLD-1 RNA binding protein. We cloned fog-2 by finding that its gene product physically interacts with GLD-1, forming a FOG-2/GLD-1/tra-2 3′untranslated region ternary complex. FOG-2 has an N-terminal F-box and a novel C-terminal domain called FTH. Canonical F-box proteins act as bridging components of the SCF ubiquitin ligase complex; the N-terminal F-box binds a Skp1 homolog, recruiting ubiquination machinery, while a C-terminal protein-protein interaction domain binds a specific substrate for degradation. However, since both fog-2 and gld-1 are necessary for spermatogenesis, FOG-2 cannot target GLD-1 for ubiquitin-mediated degradation. We propose that FOG-2 also acts as a bridge, bringing GLD-1 bound to tra-2 mRNA into a multiprotein translational repression complex, thus representing a novel function for an F-box protein. fog-2 is a member of a large, apparently rapidly evolving, C. elegans gene family that has expanded, in part, by local duplications; fog-2 related genes have not been found outside nematodes. fog-2 may have arisen during evolution of self-fertile hermaphroditism from an ancestral female/male species.

Original languageEnglish
Pages (from-to)5265-5276
Number of pages12
JournalDevelopment
Volume127
Issue number24
StatePublished - 2000

Keywords

  • Caenorhabditis elegans
  • F-box
  • FOG-2
  • GLD-1
  • Germline sex determination
  • Tra-2 mRNA
  • Translational repression

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