Archana Bairavasundaram Prusty

ORCID: 0000-0003-4749-3175
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About
Contact & Profiles
Research Areas
  • RNA Research and Splicing
  • RNA modifications and cancer
  • RNA and protein synthesis mechanisms
  • Neurogenetic and Muscular Disorders Research
  • Cytomegalovirus and herpesvirus research
  • Cancer-related gene regulation
  • RNA regulation and disease
  • Nuclear Receptors and Signaling
  • Magnetism in coordination complexes
  • Metal complexes synthesis and properties
  • Genomics and Chromatin Dynamics
  • Circular RNAs in diseases
  • Viral Infections and Immunology Research
  • Epigenetics and DNA Methylation
  • MicroRNA in disease regulation
  • Cancer-related molecular mechanisms research
  • interferon and immune responses
  • Organometallic Compounds Synthesis and Characterization

University of Würzburg
2017-2024

European Molecular Biology Organization
2011

RNA helicases constitute a large protein family implicated in cellular homeostasis and disease development. Here, we show that the helicase IGHMBP2, linked to neuromuscular disorder spinal muscular atrophy with respiratory distress type 1 (SMARD1), associates polysomes impacts translation of mRNAs containing short, GC-rich, structured 5′ UTRs. The absence IGHMBP2 causes ribosome stalling at start codon target mRNAs, leading reduced efficiency. main mRNA targets IGHMBP2-mediated regulation...

10.1016/j.celrep.2024.113802 article EN cc-by Cell Reports 2024-02-01

Abstract Spliceosomal snRNPs are multicomponent particles that undergo a complex maturation pathway. Human Sm-class snRNAs generated as 3′-end extended precursors, which exported to the cytoplasm and assembled together with Sm proteins into core RNPs by SMN complex. Here, we provide evidence these pre-snRNA substrates contain compact, evolutionarily conserved secondary structures overlap binding site. These structural motifs in pre-snRNAs predicted interfere assembly. We model rearrangements...

10.1038/s41467-023-42324-0 article EN cc-by Nature Communications 2023-10-18

Specialized assembly factors facilitate the formation of many macromolecular complexes in vivo. The Sm core structures spliceosomal U-rich small nuclear ribonucleoprotein particles (UsnRNPs) requires united protein arginine methyltransferase 5 (PRMT5) and survival motor neuron (SMN) complexes. We demonstrate that perturbations this machinery trigger complex cellular responses prevent aggregation unassembled proteins. Inactivation SMN results initial tailback proteins on PRMT5 complex,...

10.1083/jcb.201611108 article EN cc-by-nc-sa The Journal of Cell Biology 2017-06-21

Malfunction of pre-mRNA processing factors are linked to several human diseases including cancer and neurodegeneration. Here we report the identification a de novo heterozygous missense mutation in SNRPE gene (c.65T>C (p.Phe22Ser)) patient with non-syndromal primary (congenital) microcephaly intellectual disability. encodes SmE, basal component U snRNPs. We show that microcephaly-linked SmE variant is unable interact SMN complex as consequence fails assemble into This results widespread mRNA...

10.1371/journal.pgen.1008460 article EN cc-by PLoS Genetics 2019-10-31

RNA helicases constitute a large protein family implicated in cellular homeostasis and disease development. Here we show that the helicase Ighmbp2, linked to neuromuscular disorder SMARD1 associates with polysomes impacts on translation of mRNAs containing short, GC-rich highly structured 5’UTRs. Absence Ighmbp2 causes ribosome stalling at start codon target mRNAs, leading their reduced efficiency. The main mRNA targets Ighmbp2mediated regulation encode for components THO complex link...

10.2139/ssrn.4531945 preprint EN 2023-01-01

Abstract Herpesviruses have mastered host cell modulation and immune evasion to augment productive infection, life-long latency reactivation thereof 1,2. A long appreciated, yet elusively defined relationship exists between the lytic-latent switch viral non-coding RNAs 3,4. Here, we identify miRNA-mediated inhibition of miRNA processing as a novel cellular mechanism that human herpesvirus 6A (HHV-6A) exploits disrupt mitochondrial architecture, evade intrinsic defense drive latent-lytic...

10.21203/rs.3.rs-820696/v1 preprint EN cc-by Research Square (Research Square) 2021-09-03
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