ArticleNucleic acids research2022
Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- The RNA-binding protein RRP1 brakes macrophage one-carbon metabolism to suppress autoinflammation.Nature communications · 2025Article
- A higher order PUF complex is central to regulation of C. elegans germline stem cells.Nature communications · 2025Article
- A higher order PUF complex is central to regulation ofbioRxiv : the preprint server for biology · 2024Article
- PUF partner interactions at a conserved interface shape the RNA-binding landscape and cell fate in Caenorhabditis elegans.Developmental cell · 2024Article
- Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding.Nature communications · 2023Article
- The in vivo functional significance of PUF hub partnerships in C. elegans germline stem cells.Development (Cambridge, England) · 2023Article
- Functional significance of PUF partnerships inbioRxiv : the preprint server for biology · 2023Article
- Oogenesis in Caenorhabditis elegans.Sexual development : genetics, molecular biology, evolution, endocrinology, embryology, and pathology of sex determination and differentiation · 2023Review
- RNA-binding proteins in pain.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, modulates mRNA regulation by the PUF protein, FBF-2. LST-1 contains two nonidentical sites of interaction with FBF-2, LST-1 A and B. Our crystal structures of complexes of FBF-2, LST-1 A, and RNA visualize how FBF-2 associates with LST-1 A versus LST-1 B. One commonality is that FBF-2 contacts the conserved lysine and leucine side chains in the KxxL motifs in LST-1 A and B. A key difference is that FBF-2 forms unique contacts with regions N- and C-terminal to the KxxL motif. Consequently, LST-1 A does not modulate the RNA-binding affinity of FBF-2, whereas LST-1 B decreases RNA-binding affinity of FBF-2. The N-terminal region of LST-1 B, which binds near the 5' end of RNA elements, is essential to modulate FBF-2 RNA-binding affinity, while the C-terminal residues of LST-1 B contribute strong binding affinity to FBF-2. We conclude that LST-1 has the potential to impact which mRNAs are regulated depending on the precise nature of engagement through its functionally distinct FBF binding sites.
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