Abstract
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.
Keywords: trna, ribozyme, aminoglycosides, peptidyl transferase, psoriasis, retinoids, calcipotriol, anthralin
Current Medicinal Chemistry
Title: RNase P: A Promising Molecular Target for the Development of New Drugs
Volume: 11 Issue: 22
Author(s): Apostolos Tekos, Constantinos Stathopoulos, Dionysios Tsambaos and Denis Drainas
Affiliation:
Keywords: trna, ribozyme, aminoglycosides, peptidyl transferase, psoriasis, retinoids, calcipotriol, anthralin
Abstract: 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.
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Cite this article as:
Tekos Apostolos, Stathopoulos Constantinos, Tsambaos Dionysios and Drainas Denis, RNase P: A Promising Molecular Target for the Development of New Drugs, Current Medicinal Chemistry 2004; 11 (22) . https://dx.doi.org/10.2174/0929867043364054
DOI https://dx.doi.org/10.2174/0929867043364054 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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