Results 51 to 60 of about 455,663 (298)
Archaeal RNase P has multiple protein subunits homologous to eukaryotic nuclear RNase P proteins [PDF]
Although archaeal RNase P RNAs are similar in both sequence and structure to those of Bacteria rather than eukaryotes, and heterologous reconstitution between the Bacillus subtilis RNase P protein and some archaeal RNase P RNAs has been demonstrated, no archaeal protein sequences with similarity to any known bacterial RNase P protein subunit have been ...
Thomas A, Hall, James W, Brown
openaire +2 more sources
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions
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]
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
A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags
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
doaj +1 more source
RNA synthesis in mitochondria isolated from rat liver [PDF]
Mitochondrial RNA (mtRNA) was synthesized from purine and pyrimidine nucleosides in coupling with oxidative phosphorylation using isolated mitochondria. The in vivo synthesized mtRNA was adenine-uracil rich and sedimented at about 20 S by sucrose density
Inaba, Kozo, Oda, Takuzo
core +1 more source
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]
[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
RNase P Ribozymes Inhibit the Replication of Human Cytomegalovirus by Targeting Essential Viral Capsid Proteins. [PDF]
An engineered RNase P-based ribozyme variant, which was generated using the in vitro selection procedure, was used to target the overlapping mRNA region of two proteins essential for human cytomegalovirus (HCMV) replication: capsid assembly protein (AP ...
LIU, Fenyong +9 more
core +3 more sources
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
Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang +8 more
wiley +1 more source

