Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.14/45520
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- Title
- And now we are 8 : protein recruitment by LSM rings within RNPS
- Related
- ComBio2006 Conference (24 - 28 September 2006 : Brisbane)
- Related
- ComBio 2006 : combined conference abstracts, p.47
- Related
- Proceedings of the Australian Society for Biochemistry and Molecular Biology Vol. 38
- Publisher
- Kent Town, SA : Australian Society for Biochemistry and Molecular Biology
- Date
- 2006
- FoR/RFCD Code(s)
-
270199 Biochemistry and Cell Biology not elsewhere classified
- Author/Creator
- Naidoo, N
- Author/Creator
- Sobti, M
- Author/Creator
- Harrop, S. J
- Author/Creator
- Curmi, P. M. G
- Author/Creator
- Mabbutt, B. C
- Description
- 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].
- Description
- 1 page(s)
- Subject Keyword
- 270199 Biochemistry and Cell Biology not elsewhere classified
- Resource Type
- conference paper abstract
- Organisation
- Macquarie University. Dept. of Chemistry and Biomolecular Sciences
- Identifier
- http://hdl.handle.net/1959.14/45520
- Identifier
- ISSN:1328-4924
- Identifier
- mq-rm-2006000596
- Language
- eng
