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Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects

Opened Access Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects

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Autor: Vioque Peña, Agustín
Lai, Lien B.
Kirsebom, Leif A
Gopalan, Venkat
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2010
Publicado en: FEBS Letters, 584 (2), 287-296.
Tipo de documento: Artículo
Resumen: 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.
Cita: Vioque Peña, A., Lai, L.B., Kirsebom, L.A. y Gopalan, V. (2010). Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects. FEBS Letters, 584 (2), 287-296.
Tamaño: 830.4Kb
Formato: PDF

URI: http://hdl.handle.net/11441/67615

DOI: 10.1016/j.febslet.2009.11.048

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