Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1

被引：1
|
作者：
Kozlov, Guennadi [1 ,2 ]
Jiang, Jianning [1 ,2 ]
Rutherford, Tyler [3 ]
Noronha, Anne M. [3 ]
Wilds, Christopher J. [3 ]
Gehring, Kalle [1 ,2 ]
机构：
[1] McGill Univ, Dept Biochem, 3649 Promenade Sir William Osler, Montreal, PQ H3G0B1, Canada
[2] McGill Univ, Ctr Rech Biol Struct, Montreal, PQ, Canada
[3] Concordia Univ, Dept Chem & Biochem, Montreal, PQ, Canada
来源：
RNA BIOLOGY | 2024年 / 21卷 / 01期
基金：
美国国家卫生研究院; 加拿大健康研究院; 美国国家科学基金会; 加拿大自然科学与工程研究理事会; 加拿大创新基金会;
关键词：
LaM; La motif; LARP; La-related protein; LARP1; La-related protein 1; poly(a) tail; guanylation; phosphorothioate; STRUCTURAL-ANALYSIS; PROTEIN LARP1; TRANSLATION; MOTIF; RECOGNITION; MTOR; MECHANISM; FEATURES;
D O I：
10.1080/15476286.2024.2379121
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：7 / 16
页数：10
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