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UID:submissions.pasc-conference.org_PASC24_sess167_msa305@linklings.com
SUMMARY:Multiscale Simulations of Molecular Recognition by Phase Separated
  MUT-16: A Scaffolding Protein of Mutator Foci
DESCRIPTION:Minisymposium\n\nKumar Gaurav (Johannes Gutenberg University M
 ainz; Institue of Molecular Biology, Mainz)\n\nPhase-separated condensates
  play a pivotal role in organizing biomolecular interactions within cells.
  In the context of the RNA silencing pathway, crucial for gene expression 
 regulation and defense against foreign nucleic acids in organisms like C. 
 elegans, Mutator foci serve as perinuclear germ granules facilitating siRN
 A amplification. The scaffolding protein MUT-16 orchestrates the assembly 
 of Mutator complexes within these foci, with the exoribonuclease MUT-7 and
  bridging protein MUT-8 being key components. Despite the known role of MU
 T-8 in facilitating MUT-7 recruitment, the mechanism of its binding to MUT
 -16 remains elusive. Through multi-scale molecular dynamics simulations an
 d in vitro experiments, we elucidated the molecular underpinnings of MUT-1
 6 phase separation and MUT-8 recruitment. Coarse-grained simulations revea
 led the phase separation propensities of MUT-16 disordered regions, valida
 ted by experiments. Additionally, aromatic amino acids, particularly Tyr a
 nd Phe, were identified as essential for MUT-16 phase separation. Atomisti
 c simulations unveiled the crucial cation-π interactions between Tyr resid
 ues of MUT-8 and Arg/Lys residues of MUT-16, highlighting the superiority 
 of Arg-Tyr interactions over Lys-Tyr interactions in MUT-8 recruitment, as
  corroborated by in vitro mutagenesis experiments. Our findings provide va
 luable insights into the intricate molecular mechanisms governing biomolec
 ular recruitment within phase-separated condensates.\n\nDomain: Chemistry 
 and Materials, Life Sciences, Physics\n\nSession Chair: Andreas Vitalis (U
 niversity of Zurich)
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