Results 181 to 190 of about 4,319 (202)

LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria [PDF]

open access: yesNucleic Acids Research, 2012
In human mitochondria, 10 mRNAs species are generated from a long polycistronic precursor that is transcribed from the heavy chain of mitochondrial DNA, in theory yielding equal copy numbers of mRNA molecules. However, the steady-state levels of these mRNAs differ substantially.
Takeshi Chujo   +2 more
exaly   +3 more sources

The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines [PDF]

open access: yesJournal of Biomedical Science, 2007
The structure and function of polynucleotide phosphorylase (PNPase) and the exosome, as well as their associated RNA-helicases proteins, are described in the light of recent studies. The picture raised is of an evolutionarily conserved RNA-degradation machine which exonucleolytically degrades RNA from 3' to 5'.
Sue Lin-Chao, Gadi Schuster
exaly   +3 more sources
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Biochemical characterization of Campylobacter jejuni PNPase, an exoribonuclease important for bacterial pathogenicity

Biochimie, 2018
Bacteria need to promptly respond to environmental changes. Ribonucleases (RNases) are key factors in the adaptation to new environments by enabling a rapid adjustment in RNA levels. The exoribonuclease polynucleotide phosphorylase (PNPase) is essential for low-temperature cell survival, affects the synthesis of proteins involved in virulence and has ...
Casinhas, Jorge   +3 more
openaire   +3 more sources

Polynucleotide phosphorylase (PNPase) is required for Salmonella enterica serovar Typhimurium colonization in swine

Microbial Pathogenesis, 2013
The pnp gene encodes polynucleotide phosphorylase, an exoribonuclease involved in RNA processing and degradation. A mutation in the pnp gene was previously identified by our group in a signature-tagged mutagenesis screen designed to search for Salmonella enterica serovar Typhimurium genes required for survival in an ex vivo swine stomach content assay.
S M D, Bearson   +3 more
openaire   +2 more sources

A conserved loop in polynucleotide phosphorylase (PNPase) essential for both RNA and ADP/phosphate binding

Biochimie, 2014
Polynucleotide phosphorylase (PNPase) reversibly catalyzes RNA phosphorolysis and polymerization of nucleoside diphosphates. Its homotrimeric structure forms a central channel where RNA is accommodated. Each protomer core is formed by two paralogous RNase PH domains: PNPase1, whose function is largely unknown, hosts a conserved FFRR loop interacting ...
Carzaniga, T   +8 more
openaire   +3 more sources

PNPase modulates RNase II expression in Escherichia coli: implications for mRNA decay and cell metabolism

Molecular Microbiology, 1996
Summary PNPase and RNase II are the key regulatory exo‐nucleases controlling mRNA decay in Escherichia coli The rnb transcripts were found to proceed through the terminator and PNPase was found to be involved in the 3’to 5’degradation of rnb mRNA. Analysis of these longer 3’termini revealed that they are located in UA‐rich regions. Comparison of single
R, Zilhão   +3 more
openaire   +2 more sources

Modular domain organization of RNase E and PNPase

2009
mRNA decay in Escherichia coli is carried out and controlled by concerted actions of a number of ribonucleases and other protein factors. In order to gain insights into the catalytic mechanisms and regulation involved in this important cellular process, we have utilized mutational analysis to study two key enzymes, RNase E and PNPase.
openaire   +1 more source

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