The oligomeric state of archaeal fibrillarin : implications in the organization and function of essential box C/D sRNP particles

Several vital cellular processes are preformed by large ribonucleoprotein (RNP) complexes. In archaeal and eukaryotic cells one example of these essential RNP particles is the box C/D sRNP. In archaea, this complex is responsible for methylation of ribosomal RNA (rRNA) and transfer RNA (tRNA) during their maturation. Archaeal fibrillarin (aFib) is the 2'-O methyltransferase responsible for catalysis by this complex. In this work we have identified the ability of aFib from Sulfolobus acidocaldarius to form dimers at biologically relevant concentrations and the structural determinants essential for this association. Based on our model we have predicted the ability of aFibs to form dimers in different archaeal and eukaryotic species. The ability of aFibs and their eukaryotic homologs to potentially adopt multiple conformations provides insight into the dynamics of the box C/D sRNP complex. As observed in the study of other essential RNP particles, the ability of these complexes to be conformationally diverse is integral to efficient catalysis of their varied substrates.

Authors

• Burke, Paula Louise
• University of Lethbridge. Faculty of Arts and Science

• Dissertations, Academic
• Archaebacteria -- Molecular aspects
• Nucleoproteins
• Eukaryotic cells

Identifier

hdl:10133/540

OAI identifier oai:identifier

oai:opus.uleth.ca:10133/540