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. Author manuscript; available in PMC: 2025 Jan 1.
Published in final edited form as: Trends Biochem Sci. 2023 Dec 14;49(1):12–27. doi: 10.1016/j.tibs.2023.10.008

Table 2.

Pseudouridine-sensitive RNA-protein interactions.

Pseudouridine-sensitive protein-RNA interactions
Protein Level of Evidence Effects Hypothesized
Function of Ψ
References
RNase L Fully Ψ-substituteda exogenous mRNA delivered to mammalian cells - Prevent RNA degradation [60]
RNase E Artificialb single Ψ in vitro - Prevent RNA degradation [61]
PRP5 Ψ removal by writer enzyme deletion in yeast Ψ increased binding presumably through structure effects Spliceosome assembly [69]
MetRS In vitro oligo binding assay and in vivo Ψ-to-C mutation in yeast Ψ increased binding Translation [64]
U2AF2 Artificial substitution of Ψ at specific locations of polypyrimidine tract in vitro Ψ decreased binding due to rigidification of backbone Splice site recognition [65]
MBNL1 Artificial addition of Ψ in binding site in vitro[67] Ψ decreased binding due to rigidification of backbone - [67]
PUM2 Artificial addition of Ψ in binding site in vitro[68] Ψ decreased binding - [68]
RIG-I Fully Ψ substituted RNA in vitro Ψ increased binding and suppressed filament formation[62,63] Prevent innate immune activation [62,63]
a -

Fully Ψ-substituted = 100% of U’s replaced with Ψ during in vitro transcription.

b -

Artificial Ψ = Ψ has not been demonstrated to exist in endogenous contexts, but site-specific and 100% modified at that location.