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PubMed Publications| Keyword search (4,163 papers available) |  |
"Noronha AM" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1 | Kozlov G; Jiang J; Rutherford T; Noronha AM; Wilds CJ; Gehring K; | 39016322 CHEMBIOCHEM |
| 2 | Structural basis of 3'-end poly(A) RNA recognition by LARP1 | Kozlov G; Mattijssen S; Jiang J; Nyandwi S; Sprules T; Iben JR; Coon SL; Gaidamakov S; Noronha AM; Wilds CJ; Maraia RJ; Gehring K; | 35979957 CHEMBIOCHEM |
| 3 | Hydrated electrons induce the formation of interstrand cross-links in DNA modified by cisplatin adducts | Behmand B; Noronha AM; Wilds CJ; Marignier JL; Mostafavi M; Wagner JR; Hunting DJ; Sanche L; | 32211848 CHEMBIOCHEM |
| 4 | O4-alkyl-2'-deoxythymidine cross-linked DNA to probe recognition and repair by O6-alkylguanine DNA alkyltransferases. | McManus FP, O'Flaherty DK, Noronha AM, Wilds CJ | 22850722 CHEMBIOCHEM |
| 5 | Preparation of covalently linked complexes between DNA and O(6)-alkylguanine-DNA alkyltransferase using interstrand cross-linked DNA. | McManus FP, Khaira A, Noronha AM, Wilds CJ | 23347328 CHEMBIOCHEM |
| 6 | Structural basis of interstrand cross-link repair by O6-alkylguanine DNA alkyltransferase. | Denisov AY, McManus FP, O'Flaherty DK, Noronha AM, Wilds CJ | 28937154 CHEMBIOCHEM |
| 7 | Influence of nucleotide modifications at the C2' position on the Hoogsteen base-paired parallel-stranded duplex of poly(A) RNA. | Copp W, Denisov AY, Xie J, Noronha AM, Liczner C, Safaee N, Wilds CJ, Gehring K | 28973475 CHEMBIOCHEM |
| 8 | Altering Residue 134 Confers an Increased Substrate Range of Alkylated Nucleosides to the E. coli OGT Protein. | Schoonhoven NM, O'Flaherty DK, McManus FP, Sacre L, Noronha AM, Kornblatt MJ, Wilds CJ | 29137116 CHEMBIOCHEM |
| Title: | Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1 | ||||
| Authors: | Kozlov G, Jiang J, Rutherford T, Noronha AM, Wilds CJ, Gehring K | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/39016322/ | ||||
| DOI: | 10.1080/15476286.2024.2379121 | ||||
| Publication: | RNA biology | ||||
| Keywords: | LARP, La-related protein; LARP1, La-related protein 1; LaM, La motif; guanylation; phosphorothioate; poly(a) tail; | ||||
| PMID: | 39016322 | Category: | Date Added: | 2024-07-17 | |
| Dept Affiliation: |
CHEMBIOCHEM
1 Department of Biochemistry, McGill University, Montréal, Quebec, Canada. 2 Centre de recherche en biologie structurale, McGill University, Montréal, Quebec, Canada. 3 Department of Chemistry and Biochemistry, Concordia University, Montréal, Quebec, Canada. |
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Description: |
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]. |
