8VIV

Crystal structure of FBF-2 RBD in complex with gld-1 FBEa* RNA

Summary for 8VIV

• Entry DOI: 10.2210/pdb8viv/pdb
• Descriptor: Fem-3 mRNA-binding factor 2, RNA (5'-R(*CP*AP*UP*GP*UP*UP*GP*CP*CP*AP*U)-3') (3 entities in total)
• Functional Keywords: puf protein, rna binding protein
• Biological source: Caenorhabditis elegans; More
• Total number of polymer chains: 2
• Total formula weight: 50463.13

Authors

Qiu, C.,Hall, T.M.T. (deposition date: 2024-01-05, release date: 2024-11-27, Last modification date: 2025-06-11)

Primary citation

Qiu, C.,Crittenden, S.L.,Carrick, B.H.,Dillard, L.B.,Costa Dos Santos, S.J.,Dandey, V.P.,Dutcher, R.C.,Viverette, E.G.,Wine, R.N.,Woodworth, J.,Campbell, Z.T.,Wickens, M.,Borgnia, M.J.,Kimble, J.,Hall, T.M.T.
A higher order PUF complex is central to regulation of C. elegans germline stem cells.
Nat Commun, 16:123-123, 2025

PubMed Abstract: PUF RNA-binding proteins are broadly conserved stem cell regulators. Nematode PUF proteins maintain germline stem cells (GSCs) and, with key partner proteins, repress differentiation mRNAs, including gld-1. Here we report that PUF protein FBF-2 and its partner LST-1 form a ternary complex that represses gld-1 via a pair of adjacent FBF binding elements (FBEs) in its 3'UTR. One LST-1 molecule links two FBF-2 molecules via motifs in the LST-1 intrinsically-disordered region; the gld-1 FBE pair includes a well-established 'canonical' FBE and a newly-identified noncanonical FBE. Remarkably, this FBE pair drives both full RNA repression in GSCs and full RNA activation upon differentiation. Discoveries of the LST-1-FBF-2 ternary complex, the gld-1 adjacent FBEs, and their in vivo significance predict an expanded regulatory repertoire of different assemblies of PUF-partner-RNA higher order complexes in nematode GSCs. This also suggests analogous PUF controls may await discovery in other biological contexts and organisms.

PubMed: 39747099
DOI: 10.1038/s41467-024-55526-x

Experimental method

X-RAY DIFFRACTION (2.2 Å)