Apostolos Tekos, Constantinos Stathopoulos, Dionysios Tsambaos and Denis Drainas Pages 2979 - 2989 ( 11 )
RNase P is an ubiquitous and essential endonuclease in tRNA biogenesis, which generates the mature 5-termini of tRNAs. RNase P activities have been identified in all three kingdoms of life (Bacteria, Archaea, Eukarya). Most forms of RNase P are ribonucleoproteins, i.e., they consist of an essential RNA and protein subunits. In bacteria and in some archaea, the catalytic function of this enzyme resides entirely in its RNA subunit, which is one of firstly identified ribozymes. Its high structural and functional diversity among representatives of a vast variety of phylogenetic domains indicates that RNase P could also serve as a molecular target of and a useful screening system for the biological activity of different compounds and give more insight into the molecular mechanisms of their action inside the cell. The emerged information from recent studies on the mechanism and structural idiosyncrasies of RNase P provides a convenient platform for designing specific inhibitors for this ribozyme and potential areas of its application in gene therapy. This review summarises the current information on the effect of several protein synthesis inhibitors, retinoids and arotinoids, vitamin D analogues and anthalin on the activity of RNase P.
trna, ribozyme, aminoglycosides, peptidyl transferase, psoriasis, retinoids, calcipotriol, anthralin
Department of Biochemistry, School of Medicine, University of Patras, 265 04 Patras, Greece.