The RNase P family

• Published in: RNA biology Vol. 6; no. 4; pp. 362 - 369
• Main Authors: Ellis, J. Christopher, Brown, James W.
• Format: Journal Article
• Language: English
• Published: United States Taylor & Francis 01-09-2009
• Subjects: Archaea - enzymology; Bacteria - enzymology; Base Sequence; Binding; Biology; Bioscience; Calcium; Cancer; Cell; Cycle; Eukaryota - enzymology; Landes; Molecular Sequence Data; Nucleic Acid Conformation; Organogenesis; Proteins; Ribonuclease P - genetics; Ribonuclease P - metabolism; RNA, Bacterial - chemistry; RNA, Bacterial - genetics
• ISSN: 1547-6286; 1555-8584
• DOI: 10.4161/rna.6.4.9241

Ribonuclease P (RNase P) is a ribonucleoprotein comprised of a catalytic RNA subunit and one or several protein subunits. RNase P is best known for its role in 5´-processing of tRNA precursors. RNase P enzymes from almost all forms of life, including protein-synthesizing organelles, contain an RNase P with a conserved, homologous RNA. Five distinct structure classes of RNase P RNAs have been identified in Bacteria and Archaea; eukaryotic RNase P RNAs are not yet sufficiently well surveyed for structure classes to be defined. Here we will examine the structure variations in RNase P RNAs in Bacteria, Archaea, Eukaryotes, plastids, and mitochondria with special emphasis on the functional roles these unique secondary structures perform.