Kluyveromyces lactis SEF1 and itsSaccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of theS. cerevisiae RPM2 gene

Groom, Kathleen R.; Heyman, Hong Chen; Steffen, Marlene C.; Hawkins, Laverne; Martín, Nancy

doi:10.1002/(sici)1097-0061(19980115)14:1<77::aid-yea201>3.0.co;2-p

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Cited by 16 publications

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Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre-tRNA pathway

2001

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Ribonuclease P is an ancient enzyme that cleaves pre-tRNAs to generate mature 5' ends. It contains an essential RNA subunit in Bacteria, Archaea, and Eukarya, but the degree to which the RNA subunit relies on proteins to supplement catalysis is highly variable. The eukaryotic nuclear holoenzyme has recently been found to contain almost twenty times the protein content of the bacterial enzymes, in addition to having split into at least two related enzymes with distinct substrate specificity. In this review, recent progress in understanding the molecular architecture and functions of nuclear forms of RNase P will be considered.

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