Results 1 to 10 of about 20,593,893 (291)
Solution structure of RNase P RNA [PDF]
RNA, 2011 The ribonucleoprotein enzyme ribonuclease P (RNase P) processes tRNAs by cleavage of precursor-tRNAs. RNase P is a ribozyme: The RNA component catalyzes tRNA maturation in vitro without proteins. Remarkable features of RNase P include multiple turnovers in vivo and ability to process diverse substrates.
Alexei V, Kazantsev +5 more
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RNase P RNA‐mediated cleavage [PDF]
IUBMB Life, 2009 AbstractMetal(II)‐induced hydrolysis of RNA produce products with 5′‐hydroxyls and 2′;3′‐cyclic phosphates at the ends. Ribozymes are RNA molecules that act as catalysts. Some ribozymes that cleave RNA also generate 5′‐hydroxyls and 2′;3′‐cyclic phosphates whereas others produces 5′‐phosphates and 3′‐hydroxyls at the ends of the cleavage products ...
Leif A, Kirsebom, Stefan, Trobro
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BMC Genomics, 2010 Background Effective bioinformatics solutions are needed to tackle challenges posed by industrial-scale genome annotation. We present Bcheck, a wrapper tool which predicts RNase P RNA genes by combining the speed of pattern matching and sensitivity of ...
Stadler Peter F +3 more
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A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags
Bio-Protocol, 2023 Interactions between RNA-binding proteins and RNA molecules are at the center of multiple biological processes. Therefore, accurate characterization of the composition of ribonucleoprotein complexes (RNPs) is crucial.
Violette Charteau +2 more
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Modeling the Thermoproteaceae RNase P RNA [PDF]
RNA Biology, 2012 The RNA component of the RNase P complex is found throughout most branches of the tree of life and is principally responsible for removing the 5' leader sequence from pre-tRNA transcripts during tRNA maturation. RNase P RNA has a number of universal core features, however variations in sequence and structure found in homologs across the tree of life ...
Chan, Patricia P. +2 more
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Cell Reports, 2012 RNase P is the endonuclease that removes 5′ extensions from tRNA precursors. In its best-known form, the enzyme is composed of a catalytic RNA and a protein moiety variable in number and mass. This ribonucleoprotein enzyme is widely considered ubiquitous
Andreas Taschner +5 more
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Human RNase H1 is associated with protein P32 and is involved in mitochondrial pre-rRNA processing. [PDF]
PLoS 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
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Chance and necessity in the evolution of RNase P [PDF]
RNA, 2017 RNase P catalyzes 5′-maturation of tRNAs in all three domains of life. This primary function is accomplished by either a ribozyme-centered ribonucleoprotein (RNP) or a protein-only variant (with one to three polypeptides). The large, multicomponent archaeal and eukaryotic RNase P RNPs appear disproportionate to the simplicity of their role in tRNA 5 ...
Gopalan, Venkat +2 more
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Structural and functional basis for RNA cleavage by Ire1
BMC Biology, 2011 Background The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1.
Stroud Robert M +7 more
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A Tobacco S-like RNase Inhibits Hyphal Elongation of Plant Pathogens
Molecular Plant-Microbe Interactions, 2002 Ribonuclease (RNase) NE gene expression is induced in tobacco leaves in response to Phytophthora parasitica. Using antibodies directed against RNase NE, we demonstrate that RNase NE is extracellular at the early steps of the interaction, while the fungal
Karine Hugot +4 more
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