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Unexpected diversity of RNase P, an ancient tRNA processing enzyme: Challenges and prospects
Author(s) -
Lai Lien B.,
Vioque Agustín,
Kirsebom Leif A.,
Gopalan Venkat
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.048
Subject(s) - rnase p , ribonucleoprotein , rnase mrp , transfer rna , protein subunit , enzyme , biology , rnase ph , genetics , three domain system , rna , rnase h , computational biology , biochemistry , bacteria , archaea , gene
For an enzyme functioning predominantly in a seemingly housekeeping role of 5′ tRNA maturation, RNase P displays a remarkable diversity in subunit make‐up across the three domains of life. Despite the protein complexity of this ribonucleoprotein enzyme increasing dramatically from bacteria to eukarya, the catalytic function rests with the RNA subunit during evolution. However, the recent demonstration of a protein‐only human mitochondrial RNase P has added further intrigue to the compositional variability of this enzyme. In this review, we discuss some possible reasons underlying the structural diversity of the active sites, and use them as thematic bases for elaborating new directions to understand how functional variations might have contributed to the complex evolution of RNase P.