Localized 2′-OH Acylation at Poly(A) Extends RNA Translation

The potential of coding RNAs as a general therapeutic modality is limited by their short intracellular lifetime. Here, we investigate the effects of localized post-transcriptional RNA modification on protein expression over time. While 2'-OH acylation of GFP RNA with stable adducts in the protein-coding region strongly suppressed protein expression, acylation at the poly(A) tail extended translation duration, with protein output increased by up to 8-fold at 36 h. Aryl amino acid derivatives proved to be most effective, while alkyl variants showed little effect. Preliminary mechanistic experiments point to disruption of the poly(A) helical structure as a contributing factor. Our study demonstrates the potential of post-transcriptional localized 2'-acylation as a simple molecular solution to enhance protein-expression capabilities of RNAs.

Authors

Institutions

Publication Details

Journal
Journal of the American Chemical Society
Published
2025-09-02
DOI
https://doi.org/10.1021/jacs.5c11900
Primary Topic
RNA modifications and cancer
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Localized 2′-OH Acylation at Poly(A) Extends RNA Translation

Linglan Fang, Ryuta Shioi, Eric T. Kool, Lu Xiao et al.
Journal of the American Chemical Society
RNA modifications and cancer
article

Localized 2′-OH Acylation at Poly(A) Extends RNA Translation

Linglan Fang, Ryuta Shioi, Eric T. Kool, Lu Xiao, Wenrui Zhong, Anna Lee, C. Bravo
article en

Abstract

The potential of coding RNAs as a general therapeutic modality is limited by their short intracellular lifetime. Here, we investigate the effects of localized post-transcriptional RNA modification on protein expression over time. While 2'-OH acylation of GFP RNA with stable adducts in the protein-coding region strongly suppressed protein expression, acylation at the poly(A) tail extended translation duration, with protein output increased by up to 8-fold at 36 h. Aryl amino acid derivatives proved to be most effective, while alkyl variants showed little effect. Preliminary mechanistic experiments point to disruption of the poly(A) helical structure as a contributing factor. Our study demonstrates the potential of post-transcriptional localized 2'-acylation as a simple molecular solution to enhance protein-expression capabilities of RNAs.

Journal of the American Chemical SocietyVol. 147(37)
Stanford University (US)
National Institute of General Medical Sciences
Openalex Percentile: Top 80%
RNA modifications and cancer
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Localized 2′-OH Acylation at Poly(A) Extends RNA Translation — Linglan Fang, Ryuta Shioi, et al. · Journal of the American Chemical Society (2025) | TGRS Research Map | TGRS