Author:
Mura Cameron,Cascio Duilio,Sawaya Michael R.,Eisenberg David S.
Abstract
Sm proteins form the core of small nuclear ribonucleoprotein
particles (snRNPs), making them key components of several
mRNA-processing assemblies, including the spliceosome. We report the
1.75-Å crystal structure of SmAP, an Sm-like archaeal protein that
forms a heptameric ring perforated by a cationic pore. In addition to
providing direct evidence for such an assembly in eukaryotic snRNPs,
this structure (i) shows that SmAP homodimers are
structurally similar to human Sm heterodimers, (ii)
supports a gene duplication model of Sm protein evolution, and
(iii) offers a model of SmAP bound to single-stranded
RNA (ssRNA) that explains Sm binding-site specificity. The pronounced
electrostatic asymmetry of the SmAP surface imparts directionality to
putative SmAP–RNA interactions.
Publisher
Proceedings of the National Academy of Sciences
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