Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP.

RNA
Shaohua XiaoD R Engelke

Abstract

RNase P and RNase MRP are ribonucleoprotein enzymes required for 5'-end maturation of precursor tRNAs (pre-tRNAs) and processing of precursor ribosomal RNAs, respectively. In yeast, RNase P and MRP holoenzymes have eight protein subunits in common, with Pop1p being the largest at >100 kDa. Little is known about the functions of Pop1p, beyond the fact that it binds specifically to the RNase P RNA subunit, RPR1 RNA. In this study, we refined the previous Pop1 phylogenetic sequence alignment and found four conserved regions. Highly conserved amino acids in yeast Pop1p were mutagenized by randomization and conditionally defective mutations were obtained. Effects of the Pop1p mutations on pre-tRNA processing, pre-rRNA processing, and stability of the RNA subunits of RNase P and MRP were examined. In most cases, functional defects in RNase P and RNase MRP in vivo were consistent with assembly defects of the holoenzymes, although moderate kinetic defects in RNase P were also observed. Most mutations affected both pre-tRNA and pre-rRNA processing, but a few mutations preferentially interfered with only RNase P or only RNase MRP. In addition, one temperature-sensitive mutation had no effect on either tRNA or rRNA processing, consistent ...Continue Reading

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Citations

Aug 21, 2008·Proceedings of the National Academy of Sciences of the United States of America·Daniel J CoughlinDavid R Engelke
May 30, 2012·Nucleic Acids Research·Mario KrehanAstrid Schön
Sep 15, 2012·Chembiochem : a European Journal of Chemical Biology·Liudmila V PavlovaRoland K Hartmann
May 24, 2013·Nucleic Acids Research·Olga EsakovaAndrey S Krasilnikov
Jul 7, 2016·American Journal of Medical Genetics. Part a·Siham Chafai ElalaouiAbdelaziz Sefiani
May 4, 2018·Nucleic Acids Research·Anna PerederinaAndrey S Krasilnikov

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