Results 81 to 90 of about 18,946,844 (347)
A general approach to high-yield biosynthesis of chimeric RNAs bearing various types of functional small RNAs for broad applications. [PDF]
, 2015 RNA research and therapy relies primarily on synthetic RNAs. We employed recombinant RNA technology toward large-scale production of pre-miRNA agents in bacteria, but found the majority of target RNAs were not or negligibly expressed. We thus developed a
Chen, Qiu-Xia +4 more
core +2 more sources
Chance and necessity in the evolution of RNase P
RNA: A publication of the RNA Society, 2018 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).
V. Gopalan +2 more
semanticscholar +1 more source
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
doaj +1 more source
Difference between Mitochondrial RNase P and Nuclear RNase P [Letters to the Editor] [PDF]
, 2001 [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.
Attardi, Giuseppe +3 more
core
Timing molecular motion and production with a synthetic transcriptional clock [PDF]
, 2011 The realization of artificial biochemical reaction networks with unique functionality is one of the main challenges for the development of synthetic biology. Due to the reduced number of components, biochemical circuits constructed in vitro promise to be
Atkinson +34 more
core +3 more sources
RNA Biology, 2013 Ribonuclease P (RNase P) catalyzes the maturation of the 5' end of precursor-tRNAs (pre-tRNA) and is conserved in all domains of life. However, the composition of RNase P varies from bacteria to archaea and eukarya, making RNase P one of the most diverse enzymes characterized.
Michael J, Howard +6 more
openaire +2 more sources
Both kinds of RNase P in all domains of life: surprises galore
RNA: A publication of the RNA Society, 2018 RNase P, an essential housekeeping endonuclease needed for 5′-processing of tRNAs, exists in two distinct forms: one with an RNA- and the other with a protein-based active site.
C. Daniels +3 more
semanticscholar +1 more source
Mapping the evolution of mitochondrial complex I through structural variation
FEBS Letters, EarlyView.Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin +2 more
wiley +1 more source
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions
Biomolecules, 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
bioRxiv, 2018 Human mitochondrial ribonuclease P (mtRNase P) is an essential three protein complex that catalyzes the 5’ end maturation of mitochondrial precursor tRNAs (pre-tRNAs).
A. Karasik, C. Fierke, M. Koutmos
semanticscholar +1 more source