Special Issue "Function and Structure of RNase P in Fungi, Bacteria and Human Cells"
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (31 January 2016)
Prof. Dr. Denis Drainas
Department of Biochemistry, School of Medicine, University of Patras, 1 Asklipiou st., 26504 Rio-Patras, Greece
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Interests: RNase P as a target for novel inhibitors; research and development of polyamine-acidic retinoid conjugates for use as antipsoriatic drugs; activation of the ribozyme RNase P for applications in the specialized silencing of gene expression
Ribonuclease P (RNase P) is an essential endonuclease that cleaves the 5' leader sequence of precursor tRNAs during their biogenesis. Almost all forms of RNase P contain a single RNA subunit, and one (in bacteria) or more (in archaea and eukaryotes) protein subunits. In bacteria, and in some archaea, the RNA subunit is a true trans-acting ribozyme, while in eukaryotes it retains traces of catalytic activity. Recently, in higher eukaryotes, a protein only form of RNase P in mitochondria and chloroplasts has been found.
RNase P is inhibited by many different kinds of inhibitors, like, protein synthesis inhibitors, retinoids, arotinoids, porphyrins, porphines, calcipotriol and anthralin. Due to its high diversity it could be served as a suitable target for the development of new drugs in the battle against bacterial drug resistance.
The finding that the minimal substrate requirements for RNase P activity is a structure equivalent to the upper part of a precursor tRNA allowed RNase P to be used as a tool for gene silencing. Endogenous RNase P directed by external guide sequences, or M1 RNA (the RNA subunit of E. coli RNase P) linked to a guide sequence (M1GS), can cleave any target RNA. This methodology makes RNase P an important tool for RNA-mediated therapeutics.
We look forward to reading your contributions,
Prof. Dr. Denis Drainas
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