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Ribonucleases P/MRP and the Expanding Ribonucleoprotein World
Author(s) -
HernandezCid Aaron,
AguirreSampieri Sergio,
DiazVilchis Adelaida,
TorresLarios Alfredo
Publication year - 2012
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1052
Subject(s) - ribonucleoprotein , business , chemistry , biochemistry , rna , gene
One of the hallmarks of life is the widespread use of certain essential ribozymes. The ubiquitous ribonuclease P (RNase P) and eukaryotic RNase MRP are essential complexes where a structured, noncoding RNA acts in catalysis. Recent discoveries have elucidated the three‐dimensional structure of the ancestral ribonucleoprotein complex, suggested the possibility of a protein‐only composition in organelles, and even noted the absence of RNase P in a non‐free‐living organism. With respect to these last two findings, import mechanisms for RNases P/MRP into mitochondria have been demonstrated, and RNase P is present in organisms with some of the smallest known genomes. Together, these results have led to an ongoing debate regarding the precise definition of how “essential” these ribozymes truly are. © IUBMB IUBMB Life, 2012.