The oligomeric state of archaeal fibrillarin : implications in the organization and function of essential box C/D sRNP particles
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Date
2006
Authors
Burke, Paula Louise
University of Lethbridge. Faculty of Arts and Science
Journal Title
Journal ISSN
Volume Title
Publisher
Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2006
Abstract
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.
Description
viii, 74 leaves ; 29 cm.
Keywords
Dissertations, Academic , Archaebacteria -- Molecular aspects , Nucleoproteins , Eukaryotic cells