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Reference: Sobti M, et al. (2010) Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA. Biochemistry 49(11):2335-45

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Abstract


The Lsm proteins organize as hetero-heptameric ring assemblies capable of binding RNA substrates and ancillary protein factors. We have constructed simplified Lsm polyproteins that organise as multimeric ring structures as analogs of the functional Lsm complexes. The polyproteins Lsm[2+3], Lsm[4+1] and Lsm[5+6] incorporate natural sequence extensions as linker peptides between the core Lsm domains. In solution, the recombinant products organise as stable ring oligomers (75 A wide, 20 A pores) in discrete tetrameric and octameric forms. Following immobilisation, the polyproteins successfully act as affinity pull-down ligands for proteins within yeast lysate, including native Lsm proteins. Interaction partners were consistent with current models of the mixed Lsm ring assembly in vivo, but also suggest that dynamic rearrangements of Lsm protein complexes can occur. The Lsm polyprotein ring complexes were seen in gel shift assays to have a preference for U-rich RNA sequences, with tightest binding measured for Lsm[2+3] with U10. Polyprotein rings containing truncated forms of Lsm1 and Lsm4 were found to associate with translation, initiation and elongation protein factors in an RNA-dependent manner. Our findings suggest Lsm1 and/or Lsm4 can interact with translationally-active mRNA.

Reference Type
Journal Article
Authors
Sobti M, Cubeddu L, Haynes PA, Mabbutt BC
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