Results 21 to 30 of about 43,981 (239)

Functions of Conserved Domains of Human Polynucleotide Phosphorylase on RNA Oxidation. [PDF]

open access: yesInsights Biomed Res, 2019
Human polynucleotide phosphorylase (hPNPase), an exoribonuclease that is primarily localized in mitochondria, plays an important role in reducing oxidized RNA and protecting cells under oxidative stress conditions. hPNPase contains two catalytic domains (
Malla S, Li Z.
europepmc   +2 more sources

Polynucleotide phosphorylase promotes the stability and function of Hfq-binding sRNAs by degrading target mRNA-derived fragments. [PDF]

open access: yesNucleic Acids Res, 2019
In many Gram-negative and some Gram-positive bacteria, small regulatory RNAs (sRNAs) that bind the RNA chaperone Hfq have a pivotal role in modulating virulence, stress responses, metabolism and biofilm formation.
Cameron TA, Matz LM, Sinha D, De Lay NR.
europepmc   +2 more sources

The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes. [PDF]

open access: yesRNA, 2016
In all bacterial species examined thus far, small regulatory RNAs (sRNAs) contribute to intricate patterns of dynamic genetic regulation. Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein ...
Bandyra KJ   +4 more
europepmc   +2 more sources

Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA TURNOVER. [PDF]

open access: yesJ Biol Chem, 2016
Polynucleotide phosphorylase (PNPase), a 3′-to-5′ phosphorolytic exoribonuclease, is thought to be the primary enzyme responsible for turnover of Bacillus subtilis mRNA. The role of PNPase in B.
Salvo E   +4 more
europepmc   +2 more sources

Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase [PDF]

open access: bronzeNucleic Acids Research, 1976
It is already known that modification of E. coli polynucleotide phosphorylase by endogenous proteolysis induces drastic changes in both phosphorolysis and polymerisation reactions. The structural parameters of the proteolysed polynucleotide phosphorylase are described.
Annie Guissani, Claude Portier
openalex   +5 more sources

Oocyte Factors Suppress Mitochondrial Polynucleotide Phosphorylase to Remodel the Metabolome and Enhance Reprogramming

open access: yesCell Reports, 2015
Oocyte factors not only drive somatic cell nuclear transfer reprogramming but also augment the efficiency and quality of induced pluripotent stem cell (iPSC) reprogramming.
Swea-Ling Khaw   +4 more
doaj   +2 more sources

Localization of components of the RNA-degrading machine in Bacillus subtilis [PDF]

open access: yesFrontiers in Microbiology, 2016
In bacteria, the control of mRNA stability is crucial to allow rapid adaptation to changing conditions. In most bacteria, RNA degradation is catalyzed by the RNA degradosome, a protein complex composed of endo- and exoribonucleases, RNA helicases and ...
Nora Cascante-Estepa   +2 more
doaj   +3 more sources

Discrimination of RNA from DNA by polynucleotide phosphorylase. [PDF]

open access: yesBiochemistry, 2013
Polynucleotide phosphorylase (PNPase) plays synthetic and degradative roles in bacterial RNA metabolism; it is also thought to participate in bacterial DNA transactions.
Unciuleac MC, Shuman S.
europepmc   +2 more sources

RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region. [PDF]

open access: yesRNA, 2014
The endoribonuclease RNase E in a range of bacteria has a conserved N-terminal catalytic domain and a less well-conserved C-terminal tail. While the role of the C-terminal tail in the formation of the degradosome, including the interaction with the ...
Zhang JY   +6 more
europepmc   +2 more sources

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