Affinage

LSM2

U6 snRNA-associated Sm-like protein LSm2 · UniProt Q9Y333

Round 2 corrected
Length
95 aa
Mass
10.8 kDa
Annotated
2026-04-28
49 papers in source corpus 16 papers cited in narrative 16 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

LSM2 is a core subunit of two functionally distinct heteroheptameric Sm-like (LSm) rings—the nuclear LSm2-8 complex and the cytoplasmic LSm1-7 complex—that govern RNA fate through U6 snRNA stabilization, pre-mRNA splicing, and mRNA decapping. In the nucleus, the LSm2-8 ring binds the 3′-terminal oligo(U) tract of U6 snRNA, with specificity conferred by recognition of the 2′,3′-cyclic phosphate end, and assembly kinetics governed by Prp24 and 3′-end RNA processing; the intact ring is essential for U6 nuclear retention, U4/U6 duplex formation, and targeting of nuclear RNAs for decapping (PMID:10523320, PMID:17251193, PMID:29615482, PMID:32518066, PMID:40216252). LSm2 and LSm3 additionally bridge the Pat1 decapping activator to the LSm1-7 ring, directly stimulating cytoplasmic mRNA decapping (PMID:24247251, PMID:12515382). Beyond canonical RNA processing, the LSm2-8 complex mediates post-transcriptional silencing of H3K27me3-marked heterochromatic genes through XRN-2-dependent transcript degradation (PMID:32251399).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 1999 High

    The initial biochemical characterization established that human LSm proteins, including LSm2, assemble into a doughnut-shaped heptameric ring that binds the 3′ U-tract of U6 snRNA and facilitates U4/U6 duplex formation, defining LSm2 as a spliceosomal assembly factor.

    Evidence Purified recombinant complex analyzed by EM, in vitro RNA binding, and immunoprecipitation

    PMID:10523320

    Open questions at the time
    • Stoichiometry and order of subunits within the ring not resolved
    • Structural basis for selective recognition of U6 over other U-rich snRNAs unknown
  2. 2001 High

    Genetic studies in yeast showed that Lsm2 and Lsm4 directly contact Lsm8 within the nuclear ring, and that the Lsm2-8 complex acts redundantly with La protein to stabilize nascent U6 snRNA, establishing the ring topology and functional redundancy in U6 biogenesis.

    Evidence Allele-specific suppressor analysis and snRNP level quantification in yeast

    PMID:11333229

    Open questions at the time
    • Whether Lsm2-Lsm8 interaction is direct or mediated through Lsm4 not distinguished biochemically
    • Mechanism of La/Lsm redundancy not defined
  3. 2002 High

    Demonstration that LSm1-7 (but not LSm8) colocalizes with decapping enzymes in cytoplasmic P-bodies, while LSm2-8 is nuclear, resolved the long-standing question of how shared LSm2-7 subunits partition between two functionally distinct complexes.

    Evidence Immunofluorescence, FRET, and dominant-negative mutagenesis in human cells

    PMID:12515382

    Open questions at the time
    • Mechanism controlling competitive assembly of Lsm1-7 vs Lsm2-8 not yet identified
    • Whether P-body localization is required for decapping function unclear
  4. 2004 High

    Two parallel discoveries expanded LSm2 functions: the nuclear Lsm2-8 complex was shown to target nuclear-restricted mRNAs for decapping and 5′ degradation, and an Lsm2-7 sub-complex was found to associate with box H/ACA snoRNAs in nucleoli, indicating roles beyond U6 snRNA.

    Evidence UV crosslinking and RNA stability assays in yeast export mutants; in vitro reconstitution and sequential IP for snoRNP association

    PMID:15075370 PMID:15485930

    Open questions at the time
    • Substrates and specificity determinants for nuclear mRNA decapping by Lsm2-8 not defined
    • Functional consequence of Lsm2-7 association with snoRNAs not established
  5. 2007 High

    Systematic deletion and localization studies established that the intact Lsm2-8 ring is required for nuclear retention of U6 snRNA, and that Lsm1 and Lsm8 compete for shared Lsm2-7 subunits, with stress shifting the equilibrium toward cytoplasmic Lsm1-7 assembly.

    Evidence In situ hybridization of U6 in yeast lsm deletion strains; overexpression/depletion with fluorescence imaging

    PMID:17251193 PMID:18029398

    Open questions at the time
    • Signal or modification that triggers stress-dependent redistribution not identified
    • Whether U6 mislocalization upon Lsm loss is due to export or degradation not fully resolved
  6. 2011 High

    The crystal structure of the LSm5-6-7 sub-complex revealed a canonical Sm-fold hexameric ring that serves as an assembly intermediate, with NMR confirming LSm2-3 incorporation to form the full ring, resolving the assembly pathway.

    Evidence X-ray crystallography at 2.5 Å, NMR spectroscopy, pull-down assays

    PMID:22001694

    Open questions at the time
    • Full heptameric ring structure with RNA not yet available at this point
    • Kinetic control of assembly intermediate progression not addressed
  7. 2013 High

    A crystal structure of the Lsm2-3–Pat1C complex showed that Lsm2 and Lsm3 bridge Pat1 to the Lsm1-7 ring, and this sub-complex is sufficient to stimulate mRNA decapping, answering how the decapping activator is recruited.

    Evidence Crystal structure, in vitro decapping assay, structure-based mutagenesis validated in vivo in yeast

    PMID:24247251

    Open questions at the time
    • Whether Pat1-Lsm2/3 interaction is regulated or constitutive unknown
    • Structural basis for full Lsm1-7-Pat1 heptameric complex not resolved
  8. 2017 High

    Discovery that Pat1b forms a nuclear complex with Lsm2-8 bound to U6 snRNA and SART3 in Cajal bodies extended the Pat1–LSm paradigm to nuclear splicing regulation in human cells, linking Pat1b depletion to alternative splicing defects.

    Evidence Co-immunoprecipitation, immunofluorescence, RNAi, and RNA-seq in human cells

    PMID:28768202

    Open questions at the time
    • Molecular mechanism by which Pat1b-Lsm2-8 influences splice site selection not defined
    • Whether Pat1b competes with Prp24 for Lsm2-8 binding unknown
  9. 2018 High

    Structure-guided mutagenesis identified Lsm2-R63 as a critical U6-contacting residue, and demonstrated that U6 snRNA overexpression rescues lethality of all Lsm2-8 subunit deletions, proving that the sole essential function of the Lsm2-8 ring in yeast is U6 snRNA support.

    Evidence Alanine scanning across 235 pairwise combinations, high-copy suppressor analysis in yeast

    PMID:29615482

    Open questions at the time
    • Whether U6 support is the sole essential function in metazoans not tested
    • Contribution of non-essential Lsm2-8 functions (nuclear decapping, snoRNA association) to fitness unclear
  10. 2020 High

    Three key advances: cryo-EM structures revealed that 2′,3′-cyclic phosphate recognition discriminates Lsm2-8 from Lsm1-7 RNA selectivity; the Lsm2-8 complex was shown to silence H3K27me3-marked heterochromatic genes via XRN-2; and prefoldins were identified as Hsp90-dependent chaperones for Lsm2-8 assembly in plants.

    Evidence Four high-resolution cryo-EM structures with RNA-binding assays; genetic epistasis with xrn-2 and ChIP in C. elegans; co-IP and Hsp90 inhibitor studies in Arabidopsis

    PMID:32251399 PMID:32396196 PMID:32518066

    Open questions at the time
    • Whether cyclic phosphate recognition by Lsm2-8 is conserved in metazoans at structural level not confirmed
    • How Lsm2-8 is recruited specifically to H3K27me3-target transcripts unknown
    • Whether the PFD-Hsp90 axis for Lsm2-8 assembly operates in animals not tested
  11. 2025 High

    Single-molecule kinetics revealed that 3′-end processing of U6 and Prp24 cooperatively control Lsm2-8 assembly, and a mouse conditional knockout demonstrated that Lsm2 is essential for Club cell maintenance and lung epithelial homeostasis.

    Evidence CoSMoS with reconstituted components and defined RNA modifications; Club cell-specific Lsm2 knockout in mice with snRNA-seq and immunohistochemistry

    PMID:40022153 PMID:40216252

    Open questions at the time
    • Whether Prp24-dependent kinetic selection operates in human cells not shown
    • Mechanistic link between Lsm2 RNA processing functions and Club cell survival not defined

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major open questions include the structural basis of full Lsm1-7-Pat1 and Lsm2-8-Pat1b holo-complexes, how Lsm2-8 is recruited to heterochromatic transcripts, whether the sole-essential-function paradigm for U6 support extends to metazoan systems, and the molecular mechanism linking Lsm2 loss to epithelial cell fate decisions.
  • No full heptameric Lsm1-7-Pat1 or Lsm2-8-Pat1b complex structure
  • Mechanism of Lsm2-8 targeting to H3K27me3-marked transcripts unknown
  • Essential function of Lsm2-8 in metazoans not genetically delineated as in yeast

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 6 GO:0005198 structural molecule activity 3
Localization
GO:0005634 nucleus 5 GO:0005829 cytosol 2 GO:0005730 nucleolus 1
Pathway
R-HSA-8953854 Metabolism of RNA 10 R-HSA-74160 Gene expression (Transcription) 2
Partners
LSM1LSM3LSM4LSM8PAT1BPRP24SART3
Complex memberships
LSm1-7 heptameric ringLSm2-3-Pat1C complexLSm2-8 heptameric ringU4/U6.U5 tri-snRNP

Evidence

Reading pass · 16 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 Human LSm proteins (including LSm2) form a stable doughnut-shaped heteromeric complex that binds specifically to the 3'-terminal U-tract of U6 snRNA and facilitates U4/U6 RNA duplex formation in vitro; the complex does not bind the U-rich Sm sites of intact U1, U2, U4, or U5 snRNAs. Protein purification, electron microscopy, in vitro RNA binding assay, immunoprecipitation The EMBO journal High 10523320
2001 In yeast, LSM2 and LSM4 (but not other LSM genes) act as allele-specific low-copy suppressors of mutations in Lsm8p; overexpression of LSM2 increases levels of both Lsm8p and U6 snRNPs, consistent with Lsm2p and Lsm4p directly contacting Lsm8p within the Lsm2-8 ring; the entire Lsm2-8 complex acts redundantly with La protein (Lhp1p) to stabilize nascent U6 snRNA. Genetic suppressor analysis, overexpression experiments, snRNP level quantification Genetics High 11333229
2002 Human LSm1-7 proteins (not LSm8) colocalize with mRNA-degrading enzymes Dcp1/2 and Xrn1 in discrete cytoplasmic foci (P-bodies); LSm8 is excluded from these foci, delineating distinct cytoplasmic (LSm1-7) and nuclear (LSm2-8) complexes; complex formation is required for enrichment in cytoplasmic foci. Subcellular localization by immunofluorescence, FRET, co-expression of wild-type and dominant-negative LSm mutants RNA (New York, N.Y.) High 12515382
2004 The nuclear Lsm2-8p complex is required for decapping and 5' degradation of nucleus-restricted mRNAs and pre-mRNA degradation intermediates; Lsm8p (but not cytoplasmic Lsm1p) UV-crosslinks directly to nuclear poly(A)+ RNA, indicating the Lsm2-8p complex physically interacts with nuclear RNA substrates and targets them for decapping. UV crosslinking, genetic deletion analysis, RNA stability assays in yeast strains with nuclear mRNA export blocks Molecular and cellular biology High 15485930
2004 A third Lsm complex consisting of Lsm2-Lsm7 (without Lsm1 or Lsm8) associates with the box H/ACA snoRNA snR5 in yeast; in vitro reconstitution shows the 3' end of snR5 is critical for Lsm protein recognition; this Lsm2-7 complex is partially distinct from the canonical snR5 box H/ACA protein complex and localizes to nucleoli, suggesting a nucleolar function for Lsm proteins in snoRNA biogenesis. In vitro reconstitution of RNA-protein binding, glycerol gradient sedimentation, sequential immunoprecipitation, subcellular fractionation/localization Molecular biology of the cell High 15075370
2007 The complete Lsm2-8 complex is required for nuclear accumulation of U6 snRNA in yeast; loss of any single Lsm2-8 subunit causes U6 mislocalization; La protein has a smaller, indirect effect on U6 localization consistent with a chaperone role in Lsm2-8 assembly rather than direct nuclear retention. In situ hybridization of U6 snRNA in lsm deletion strains, genetic analysis Nucleic acids research High 17251193
2007 Nuclear accumulation of Lsm proteins in yeast depends on complex formation; Lsm8p plays a crucial role in nuclear localization, with its own localization most strongly influenced by Lsm2p and Lsm4p (its presumed neighbors); Lsm1p and Lsm8p act competitively to partition the shared Lsm2-7 subunits between cytoplasmic and nuclear complexes, and stress shifts Lsm proteins from nucleus to cytoplasm. Overexpression and depletion experiments, subcellular localization by fluorescence microscopy in yeast Journal of cell science High 18029398
2011 Crystal structure of the LSm5-6-7 (LSm657) assembly intermediate resolved at 2.5 Å reveals canonical Sm fold monomers arranged in a hexameric ring; NMR and pull-down experiments show that the LSm657 complex can incorporate LSm2-3 to assemble towards native LSm1-7 and LSm2-8 rings, identifying LSm657 as a functional building block on the assembly pathway. X-ray crystallography (2.5 Å), NMR spectroscopy, pull-down assays Journal of molecular biology High 22001694
2013 Lsm2 and Lsm3 bridge the interaction between the C-terminus of Pat1 (Pat1C) and the Lsm1-7 complex; crystal structure of the Lsm2-3-Pat1C complex shows three Pat1C molecules surrounding a heptameric Lsm2-3 ring in an asymmetric arrangement; the Lsm2-3-Pat1C complex stimulates mRNA decapping in vitro to a similar extent as full Lsm1-7-Pat1C; structure-based mutagenesis confirmed that Lsm2-3–Pat1C interactions are required for decapping activation in vivo. Crystal structure determination, in vitro decapping assay, RNA-binding assay, structure-based mutagenesis, yeast in vivo decapping assays Cell research High 24247251
2017 In human cells, Pat1b forms a nuclear complex with the Lsm2-8 heptamer that binds U6 snRNA and interacts with SART3 and additional U4/U6.U5 tri-snRNP components in Cajal bodies; Pat1b depletion causes alternative splicing changes (exon skipping at weak donor sites) as well as upregulation of P-body-enriched mRNAs, demonstrating dual roles for Pat1b/Lsm2-8 in nuclear splicing and cytoplasmic mRNA decay via distinct complexes. Co-immunoprecipitation, immunofluorescence, RNAi knockdown, RNA sequencing Cell reports High 28768202
2018 Structure-guided mutagenesis of the yeast Lsm2-8 ring identifies Lsm3-R69A (lethal) and Lsm2-R63A (severe growth defect) as critical RNA-binding residues that contact the 3'-terminal UUU of U6 snRNA; lethal deletions of lsm2, lsm3, lsm4, lsm5, and lsm8 are all rescued by U6 snRNA overexpression, establishing that the sole essential function of the Lsm2-8 ring in yeast is to support U6 snRNA biogenesis/function. Alanine scanning mutagenesis, high-copy suppressor analysis, genetic rescue with U6 overexpression RNA (New York, N.Y.) High 29615482
2020 High-resolution cryo-EM structures of Lsm2-8 bound to RNA show that the unique 2',3'-cyclic phosphate end of U6 snRNA is a prime determinant of Lsm2-8 specificity; Lsm5 uniquely recognizes purine bases, explaining its divergent sequence; in contrast, Lsm1-7 strongly discriminates against cyclic phosphates and prefers oligouridylate tracts with terminal purines, revealing the molecular basis for the distinct RNA selectivities of the two complexes. Cryo-EM structure determination (four high-resolution structures), RNA-binding specificity assays RNA (New York, N.Y.) High 32518066
2020 In C. elegans somatic cells, the LSM2-8 complex contributes to silencing of H3K27me3-marked heterochromatic genes by targeting their transcripts for degradation via the XRN-2 exoribonuclease; disruption of LSM2-8 stabilizes these mRNAs and coincides with a localized reduction of H3K27me3 at sensitive loci; this pathway does not require H3K9 methylation, distinguishing it from other heterochromatic RNA degradation pathways. Genetic knockdown/knockout, RNA stability assays, chromatin immunoprecipitation for H3K27me3, epistasis with xrn-2 Nature cell biology High 32251399
2020 In Arabidopsis, prefoldins (PFDs) interact with LSM2-8 complex components and are required to maintain adequate levels of the complex; LSM8 protein is a client of Hsp90, and PFD4 mediates the interaction between LSM8 and Hsp90; loss of PFDs reduces LSM8 levels and U6 snRNA levels and alters pre-mRNA splicing, establishing a PFD-Hsp90-LSM2-8 axis for spliceosomal complex proteostasis. Co-expression analysis, co-immunoprecipitation, Hsp90 inhibitor treatment, genetic mutant analysis, U6 snRNA quantification, splicing analysis Nucleic acids research Medium 32396196
2025 Using colocalization single-molecule spectroscopy, Lsm2-8 association with unprocessed U6 snRNA is highly dependent on Prp24, whereas 3'-end-processed U6 (bearing a 3'-phosphate) can rapidly recruit Lsm2-8 in the absence of Prp24; Prp24 promotes both recruitment and retention of Lsm2-8; this reveals a kinetic selection mechanism by which 3'-end modification and Prp24 coordinate efficient U6 snRNP assembly. Colocalization single-molecule spectroscopy (CoSMoS), in vitro reconstitution with modified and unmodified RNAs The Journal of biological chemistry High 40216252
2025 Club cell-specific knockout of Lsm2 in mice leads to a significant reduction in the Club cell population (particularly Chia1+/Crb1+ cells) and subsequent reduction in ciliated epithelial cells, exacerbating lung injury and inflammation caused by cigarette smoke exposure; in vitro, knockdown of Lsm2 in 16HBE cells significantly reduces cell viability. Club cell-specific conditional knockout in mice, single-nucleus RNA sequencing, multiplexed immunohistochemistry, in vitro siRNA knockdown with cell viability assay Respiratory research Medium 40022153

Source papers

Stage 0 corpus · 49 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 Towards a proteome-scale map of the human protein-protein interaction network. Nature 2090 16189514
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2005 A human protein-protein interaction network: a resource for annotating the proteome. Cell 1704 16169070
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2009 Defining the human deubiquitinating enzyme interaction landscape. Cell 1282 19615732
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2014 A proteome-scale map of the human interactome network. Cell 977 25416956
2012 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Molecular cell 973 22681889
2004 Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nature biotechnology 916 15592455
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2002 Comprehensive proteomic analysis of the human spliceosome. Nature 725 12226669
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2017 Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15. Science (New York, N.Y.) 533 28302793
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2007 Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme. Molecular cell 367 17643375
2003 Splicing double: insights from the second spliceosome. Nature reviews. Molecular cell biology 329 14685174
2012 Dynamic protein-protein interaction wiring of the human spliceosome. Molecular cell 318 22365833
2002 The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA (New York, N.Y.) 303 12515382
2002 Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA (New York, N.Y.) 301 11991638
2012 A high-throughput approach for measuring temporal changes in the interactome. Nature methods 273 22863883
2016 The cell proliferation antigen Ki-67 organises heterochromatin. eLife 265 26949251
1999 A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. The EMBO journal 260 10523320
1999 Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. The Journal of cell biology 235 10601333
2011 Next-generation sequencing to generate interactome datasets. Nature methods 200 21516116
2017 Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation. Cell 199 28781166
2001 Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics 65 11333229
2004 Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p complex. Molecular and cellular biology 57 15485930
2017 Environment-dependent regulation of spliceosome activity by the LSM2-8 complex in Arabidopsis. Nucleic acids research 43 28482101
2004 An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5. Molecular biology of the cell 37 15075370
2013 Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation. Cell research 35 24247251
2007 The Lsm2-8 complex determines nuclear localization of the spliceosomal U6 snRNA. Nucleic acids research 33 17251193
2020 Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes. RNA (New York, N.Y.) 31 32518066
2017 Dual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes. Cell reports 28 28768202
2007 Requirements for nuclear localization of the Lsm2-8p complex and competition between nuclear and cytoplasmic Lsm complexes. Journal of cell science 26 18029398
2020 LSM2-8 and XRN-2 contribute to the silencing of H3K27me3-marked genes through targeted RNA decay. Nature cell biology 19 32251399
2020 Prefoldins contribute to maintaining the levels of the spliceosome LSM2-8 complex through Hsp90 in Arabidopsis. Nucleic acids research 19 32396196
2011 Structure of the LSm657 complex: an assembly intermediate of the LSm1-7 and LSm2-8 rings. Journal of molecular biology 15 22001694
2022 The cytoplasmic LSm1-7 and nuclear LSm2-8 complexes exert opposite effects on Hepatitis B virus biosynthesis and interferon responses. Frontiers in immunology 8 36016928
2018 Defining essential elements and genetic interactions of the yeast Lsm2-8 ring and demonstration that essentiality of Lsm2-8 is bypassed via overexpression of U6 snRNA or the U6 snRNP subunit Prp24. RNA (New York, N.Y.) 8 29615482
2023 The mechanism of LSM2 in the progression of live hepatocellular carcinoma was analyzed based on bioinformatics. Medical oncology (Northwood, London, England) 5 37612479
2025 LSM2 drives glioma progression through alternative splicing dysregulation: a multi-omics approach to identify a potential therapeutic target. Frontiers in oncology 2 40365337
2025 Lsm2 is critical to club cell proliferation and its inhibition aggravates COPD progression. Respiratory research 0 40022153
2025 RNA Modifications and Prp24 Coordinate Lsm2-8 Binding Dynamics during S. cerevisiae U6 snRNP Assembly. bioRxiv : the preprint server for biology 0 40060616
2025 RNA modifications and Prp24 coordinate Lsm2-8 binding dynamics during S. cerevisiae U6 snRNP assembly. The Journal of biological chemistry 0 40216252