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A Protein⋅Protein Interaction Platform Involved in Recruitment of GLD-3 to the FBF⋅fem-3 mRNA Complex
- Wu, Joann, Campbell, Zachary T., Menichelli, Elena, Wickens, Marvin, Williamson, James R.
- Journal of Molecular Biology 2013 v.425 pp. 738-754
- Caenorhabditis elegans, RNA-binding proteins, conserved sequences, eukaryotic cells, germ cells, messenger RNA, models, point mutation, spermatogenesis
- The Pumilio and FBF (PUF) family of RNA-binding proteins interacts with protein partners to post-transcriptionally regulate mRNAs in eukaryotes. The interaction between PUF family member fem-3 binding factor (FBF) and germline development defective-3 (GLD-3) protein promotes spermatogenesis in Caenorhabditis elegans by increasing expression of the fem-3 mRNA. Defined here in these studies is the molecular basis for this critical interaction. A 10-amino-acid region within GLD-3 is required for FBF binding, while a 7-amino-acid loop in FBF between PUF repeats 7 and 8 is necessary for GLD-3 binding. These short sequences are conserved, as other FBF-binding proteins bear sequences similar to those in GLD-3 and other C. elegans PUF proteins contain sequences similar to those in FBF. The FBF-binding region of GLD-3 forms a ternary complex with FBF on the point mutation element (PME) in the fem-3 3′ untranslated region, and formation of this GLD-3⋅FBF complex does not impact the RNA-binding activity of FBF. These data raise the possibility of alternative models involving the formation of a GLD-3⋅FBF⋅RNA complex in the regulation of germline mRNAs.