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Eukaryotic ribonuclease P: Increased complexity to cope with the nuclear pre‐tRNA pathway
Author(s) -
Xiao Shaohua,
HouserScott Felicia,
Engelke David R.
Publication year - 2001
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/1097-4652(200104)187:1<11::aid-jcp1055>3.0.co;2-k
Subject(s) - archaea , rnase p , ribonuclease , transfer rna , protein subunit , enzyme , rna , biology , biochemistry , bacteria , microbiology and biotechnology , genetics , gene
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. J. Cell. Physiol. 187:11–20, 2001. © 2001 Wiley‐Liss, Inc.