Results 61 to 70 of about 430,076 (284)

RNase P — a ‘Scarlet Pimpernel’ [PDF]

open access: yesMolecular Microbiology, 1995
RNase P is responsible for the maturation of the 5′‐termini of tRNA molecules in all cells studied to date. This ribonucleoprotein has to recognize and identify its cleavage site on a large number of different precursors. This review covers what is currently known about the function of the catalytic subunit of Escherichia coli RNase P, M1 RNA, and the ...
openaire   +3 more sources

The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced [PDF]

open access: yes, 2004
We prepared some truncated and replaced P3 mutants of Escherichia coli RNase P RNA, and used them to examine the RNase P ribozyme and holoenzyme reactions of a pre-tRNA substrate.
Kanda, Naomi   +2 more
core   +1 more source

The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions

open access: yesBiomolecules, 2016
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life ...
Bradley P. Klemm   +6 more
doaj   +1 more source

Human RNase H1 is associated with protein P32 and is involved in mitochondrial pre-rRNA processing. [PDF]

open access: yesPLoS ONE, 2013
Mammalian RNase H1 has been implicated in mitochondrial DNA replication and RNA processing and is required for embryonic development. We identified the mitochondrial protein P32 that binds specifically to human RNase H1, but not human RNase H2. P32 binds
Hongjiang Wu   +4 more
doaj   +1 more source

Catalytic RNase P RNA from Synechocystis sp. cleaves the hepatitis C virus RNA near the AUG start codon [PDF]

open access: yes, 2004
Previously, we described two RNA structural motifs in the hepatitis C viral (HCV) genome that can be processed in vitro by human ribonuclease P (RNase P) enzyme [J. Biol. Chem. 277 (2002) 30606].
Alifano   +19 more
core   +1 more source

The role of ribonucleases in regulating global mRNA levels in the model organism Thermus thermophilus HB8 [PDF]

open access: yes, 2014
BACKGROUND: RNA metabolism, including RNA synthesis and RNA degradation, is one of the most conserved biological systems and has been intensively studied; however, the degradation network of ribonucleases (RNases) and RNA substrates is not fully ...
Akeo Shinkai   +7 more
core   +1 more source

miRNA‐29 regulates epidermal and mesenchymal functions in skin repair

open access: yesFEBS Letters, EarlyView.
miRNA‐29 inhibits cell‐to‐cell and cell‐to‐matrix adhesion by silencing mRNA targets. Adhesion is controlled by complex interactions between many types of molecules coded by mRNAs. This is crucial for keeping together the layers of the skin and for regenerating the skin after wounding.
Lalitha Thiagarajan   +10 more
wiley   +1 more source

Substrate structural requirements of Schizosaccharomyces pombe RNase P [PDF]

open access: yes, 1989
RNase P from Schizosaccharomyces pombe has been purified over 2000-fold. The apparent Km for two S. pombe tRNA precursors derived from the supS1 and sup3-e tRNASer genes is 20 nM; the apparent Vmax is 2.5 nM/min (supS1) and 1.1 nM/min (sup3-e ...
Drainas, Denis   +3 more
core   +1 more source

A cellular system to study responses to a collision between the transcription complex and a protein‐bound nick in the DNA template

open access: yesFEBS Letters, EarlyView.
We present the cellular transcription‐coupled Flp‐nick system allowing the introduction of a Top1‐mimicking cleavage complex (Flpcc) at a Flp recognition target site within a controllable LacZ gene. LacZ transcription leads to the collision of RNA polymerase II (RNAPII) with Flpcc, and this causes RNAPII stalling, ubiquitination, and degradation.
Petra Herring   +6 more
wiley   +1 more source

Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy [PDF]

open access: yes, 2011
Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleoprotein enzymes, which process RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some mRNAs, for RNase MRP.
Amero   +84 more
core   +3 more sources

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