RNase P: Variations and Uses [PDF]
Venkat Gopalan+2 more
core +8 more sources
Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I. [PDF]
Human RNase P has been initially described as a tRNA processing enzyme, consisting of H1 RNA and at least ten distinct protein subunits. Recent findings, however, indicate that this catalytic ribonucleoprotein is also required for transcription of small ...
Robert Reiner+3 more
doaj +19 more sources
Evolution of ribonuclease H genes in prokaryotes to avoid inheritance of redundant genes [PDF]
Background A theoretical model of genetic redundancy has proposed that the fates of redundant genes depend on the degree of functional redundancy, and that functionally redundant genes will not be inherited together.
Tomita Masaru+2 more
doaj +5 more sources
Genetic diversity of human RNase 8 [PDF]
Background Ribonuclease 8 is a member of the RNase A family of secretory ribonucleases; orthologs of this gene have been found only in primate genomes. RNase 8 is a divergent paralog of RNase 7, which is lysine-enriched, highly conserved, has prominent ...
Chan Calvin C+4 more
doaj +4 more sources
P finder: genomic and metagenomic annotation of RNase P RNA gene (rnpB) [PDF]
Background The rnpB gene encodes for an essential catalytic RNA (RNase P). Like other essential RNAs, RNase P’s sequence is highly variable. However, unlike other essential RNAs (i.e.
J. Christopher Ellis
doaj +2 more sources
The DnaJK chaperone of Bacillus subtilis post-transcriptionally regulates gene expression through the YlxR(RnpM)/RNase P complex [PDF]
To survive in harsh natural environments, translation and mRNA metabolism must be tightly and coordinately controlled, as saving biological costs increases fitness. However, the roles of protein chaperones in this control system are unclear.
Mitsuo Ogura+3 more
doaj +2 more sources
The recognition by RNase P of precursor tRNAs.
We have generated mutants of M1 RNA, the catalytic subunit of Escherichia coli RNaseP, and have analyzed their properties in vitro and in vivo. The mutations, A333----C333, A334----U334, and A333 A334----C333 U334 are within the sequence UGAAU which is complementary to the GT psi CR sequence found in loop IV of all E. coli tRNAs.
Madeline F. Baer+5 more
openalex +4 more sources
Varieties of RNase P: A nomenclature problem? [PDF]
Twenty-five years ago, a basic tenet of biochemistry held that enzymes are made solely of protein. Ribosomes, which are large ribonucleoprotein enzymes, were conveniently overlooked (but see Woese, 1967; Crick, 1968; Orgel, 1968). The then current orthodoxy was first challenged by the discovery that Escherichia coli RNase P had an essential RNA subunit
Sidney Altman+2 more
openalex +5 more sources
Dissecting Monomer-Dimer Equilibrium of an RNase P Protein Provides Insight Into the Synergistic Flexibility of 5’ Leader Pre-tRNA Recognition [PDF]
Ribonuclease P (RNase P) is a universal RNA-protein endonuclease that catalyzes 5’ precursor-tRNA (ptRNA) processing. The RNase P RNA plays the catalytic role in ptRNA processing; however, the RNase P protein is required for catalysis in vivo and ...
Danyun Zeng+4 more
doaj +2 more sources
Difference between Mitochondrial RNase P and Nuclear RNase P [Letters to the Editor] [PDF]
[Discussion of: Puranam, R. S., and G. Attardi. 2001. The RNase P associated with HeLa cell mitochondria contains an essential RNA component identical in sequence to that of the nuclear RNase P. Mol. Cell. Biol. 21:548-561.]
Rossmanith, Walter+3 more
openaire +4 more sources