ArticleRNA biology2024
Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1.
Article in RNA biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Poly(A) variants supporting robust transmission stability in bacteria and high protein expression in animals for mRNAMolecular therapy. Nucleic acids · 2026Article
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- LARP1 binds ribosomes and TOP mRNAs in repressed complexes.The EMBO journal · 2024Article
- Conserved Functions of LARP1 Proteins in Eukaryotes.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
6 authors.
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Abstract
La-related proteins (LARPs) are a family of RNA-binding proteins that share a conserved La motif (LaM) domain. LARP1 plays a role in regulating ribosomal protein synthesis and stabilizing mRNAs and has a unique structure without an RNA binding RRM domain adjoining the LaM domain. In this study, we investigated the physical basis for LARP1 specificity for poly(A) sequences and observed an unexpected bias for sequences with single guanines. Multiple guanine substitutions did not increase the affinity, demonstrating preferential recognition of singly guanylated sequences. We also observed that the cyclic di-nucleotides in the cCAS/STING pathway, cyclic-di-GMP and 3',3'-cGAMP, bound with sub-micromolar affinity. Isothermal titration measurements were complemented by high-resolution crystal structures of the LARP1 LaM with six different RNA ligands, including two stereoisomers of a phosphorothioate linkage. The selectivity for singly substituted poly(A) sequences suggests LARP1 may play a role in the stabilizing effect of poly(A) tail guanylation. [Figure: see text].
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