Results 11 to 20 of about 455,663 (298)
RNase P: Beyond Precursor tRNA Processing. [PDF]
Abstract Ribonuclease P (RNase P) was first described in the 1970’s as an endoribonuclease acting in the maturation of precursor transfer RNAs (tRNAs). More recent studies, however, have uncovered non-canonical roles for RNase P and its components.
Wang P, Lin J, Zheng X, Xu X.
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Potential Applications of RNase P Ribozyme Against Hepatitis B Virus [PDF]
Nucleic acid-based gene-interfering molecules, such as antisense oligonucleotides, ribozymes, and small interfering RNA (siRNA), represent exciting gene-targeting agents for therapeutic applications.
Thomas Sorrell, Yujun Liu, Fenyong Liu
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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
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A novel experimental approach for the selective isolation and characterization of human RNase MRP
RNase MRP is a ribonucleoprotein complex involved in the endoribonucleolytic cleavage of different RNAs. Mutations in the RNA component of the RNP are the cause of cartilage hair hypoplasia.
Merel Derksen +5 more
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Ribonuclease P (RNase P) is a ribonucleoprotein comprised of a catalytic RNA subunit and one or several protein subunits. RNase P is best known for its role in 5'-processing of tRNA precursors. RNase P enzymes from almost all forms of life, including protein-synthesizing organelles, contain an RNase P with a conserved, homologous RNA.
J Christopher, Ellis, James W, Brown
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The Bacillus subtilis RNase P holoenzyme contains two RNase P RNA and two RNase P protein subunits [PDF]
Ribonuclease P (RNase P) catalyzes the 5' maturation of precursor tRNA transcripts and, in bacteria, is composed of a catalytic RNA and a protein. We investigated the oligomerization state and the shape of the RNA alone and the holoenzyme of Bacillus subtilis RNase P in the absence of substrate by synchrotron small-angle X-ray scattering and affinity ...
X W, Fang +7 more
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Silencing Antibiotic Resistance with Antisense Oligonucleotides
Antisense technologies consist of the utilization of oligonucleotides or oligonucleotide analogs to interfere with undesirable biological processes, commonly through inhibition of expression of selected genes.
Saumya Jani +2 more
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A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme
RNase P, an RNA-protein complex, is essential for processing tRNAs. Three of the ten protein subunits of Saccharomyces cerevisiae RNase P (and a related complex, RNase MRP) co-purify with yeast telomerase, another RNA-protein complex.
P. Daniela Garcia, Virginia A. Zakian
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Difference between Mitochondrial RNase P and Nuclear RNase P [PDF]
We previously demonstrated that mammalian cells contain at least two distinct RNase P activities, one nuclear and one mitochondrial (5, 7). These enzymes were shown to have different substrate specificities and distinct molecular and enzymatic properties (5–7).
Walter Rossmanith, Thomas Potuschak
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RNase P RNA‐mediated cleavage [PDF]
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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