And now we are 8: protein recruitment by LSM rings within RNPS

N. Naidoo, M. Sobti, S. J. Harrop, P. M. G. Curmi, B. C. Mabbutt

Research output: Contribution to journalMeeting abstract

Abstract

Sm and Sm-like (Lsm) proteins are core components of ribonucleoprotein complexes essential to key nucleic acid processing events such as pre-mRNA splicing, mRNA degradation and histone processing. The proteins assemble as multi-unit ring scaffolds that bind RNA substrates and other necessary protein factors. Our recent crystal structure of the octameric yeast Lsm3 ring, alongside solution NMR studies, reveals a new organization for these proteins, as well as a mechanism for recruitment of other protein components to the RNP scaffold. In vivo, seven Lsm proteins form hetero-complexes, the exact components of which dictate their specific biological function. By engineering appropriate polyproteins, we have now begun to probe the structural and functional features of both mRNA-degrading Lsm[1-7] complex, as well as the U6 component Lsm[2-8].
Original languageEnglish
Pages (from-to)47
Number of pages1
JournalComBio 2006 : combined conference abstracts
Publication statusPublished - 2006
EventComBio2006 Conference - Brisbane
Duration: 24 Sep 200628 Sep 2006

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