7k3l
Crystal structure of dLC8 in complex with Panoramix TQ peptide
Structural highlights
FunctionDYL1_DROME Acts as a non-catalytic accessory component of a dynein complex (By similarity). Publication Abstract from PubMedNuclear Argonaute proteins, guided by their bound small RNAs to nascent target transcripts, mediate cotranscriptional silencing of transposons and repetitive genomic loci through heterochromatin formation. The molecular mechanisms involved in this process are incompletely understood. Here, we show that the SFiNX complex, a silencing mediator downstream from nuclear Piwi-piRNA complexes in Drosophila, facilitates cotranscriptional silencing as a homodimer. The dynein light chain protein Cut up/LC8 mediates SFiNX dimerization, and its function can be bypassed by a heterologous dimerization domain, arguing for a constitutive SFiNX dimer. Dimeric, but not monomeric SFiNX, is capable of forming molecular condensates in a nucleic acid-stimulated manner. Mutations that prevent SFiNX dimerization result in loss of condensate formation in vitro and the inability of Piwi to initiate heterochromatin formation and silence transposons in vivo. We propose that multivalent SFiNX-nucleic acid interactions are critical for heterochromatin establishment at piRNA target loci in a cotranscriptional manner. Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex.,Schnabl J, Wang J, Hohmann U, Gehre M, Batki J, Andreev VI, Purkhauser K, Fasching N, Duchek P, Novatchkova M, Mechtler K, Plaschka C, Patel DJ, Brennecke J Genes Dev. 2021 Mar 1;35(5-6):392-409. doi: 10.1101/gad.347989.120. Epub 2021 Feb , 11. PMID:33574069[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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