Results 11 to 20 of about 5,147 (230)

Lack of PNPase activity in Enterococcus faecalis 14 increases the stability of EntDD14 bacteriocin transcripts [PDF]

Scientific Reports, 2023
A mutant deficient in polynucleotide phosphorylase (PNPase) activity was previously constructed in Enterococcus faecalis 14; a strain producing a leaderless two-peptide enterocin DD14 (EntDD14).
Rabia Ladjouzi, Anca Lucau-Danila, Paloma López, Djamel Drider   +3 more
doaj   +7 more sources

Selective 8-oxo-rG stalling occurs in the catalytic core of polynucleotide phosphorylase (PNPase) during degradation. [PDF]

Proc Natl Acad Sci U S A
Significance Polynucleotide phosphorylase (PNPase) is a widely conserved exoribonuclease that degrades single-stranded RNA transcripts in the 3′ to 5′ direction, forming single-nucleotide diphosphates and a short oligonucleotide product.
Miller LG, Kim W, Schowe S, Taylor K, Han R, Jain V, Park R, Sherman M, Fang J, Ramirez H, Ellington A, Tamamis P, Resendiz MJE, Zhang YJ, Contreras L.   +14 more
europepmc   +6 more sources

Structural insights into human PNPase in health and disease. [PDF]

Nucleic Acids Res
Human polynucleotide phosphorylase (hPNPase) is a 3′-to-5′ exoribonuclease located in mitochondria, where it plays crucial roles in RNA degradation and RNA import.
Li YC, Wang CH, Patra M, Chen YP, Yang WZ, Yuan HS.   +5 more
europepmc   +6 more sources

Regulation and functions of bacterial PNPase [PDF]

Wiley Interdisciplinary Reviews RNA, 2016
Polynucleotide phosphorylase (PNPase) is an exoribonuclease that catalyzes the processive phosphorolytic degradation of RNA from the 3′‐end. The enzyme catalyzes also the reverse reaction of polymerization of nucleoside diphosphates that has been implicated in the generation of heteropolymeric tails at the RNA 3′‐end. The enzyme is widely conserved and
Federica Briani, Thomas Carzaniga, Gianni Dehò   +2 more
exaly   +7 more sources

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

Nucleic 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, Tsutomu Suzuki
exaly   +4 more sources

Pathological PNPase variants with altered RNA binding and degradation activity affect the phenotype of bacterial and human cell models. [PDF]

NAR Mol Med
Human PNPase (hPNPase) is an essential RNA exonuclease located in mitochondria, where it contributes to RNA import from the cytoplasm, degradation of mitochondrial RNA, and R-loop homeostasis. Biallelic mutations in the hPNPase PNPT1 gene cause different
Pizzoccheri R, Falchi FA, Alloni A, Caldarulo M, Camboni T, Zambelli F, Pavesi G, Visentin C, Camilloni C, Sertic S, Briani F.   +10 more
europepmc   +4 more sources

A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation [PDF]

Molecular Cell, 2021
Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic ...
Tom Dendooven, Dhriti Sinha, Alzbeta Roeselová, Todd A. Cameron, Nicholas R. De Lay, Ben F. Luisi, Katarzyna Bandyra   +6 more
semanticscholar   +4 more sources

PNPASE Regulates RNA Import into Mitochondria [PDF]

Cell, 2010
RNA import into mammalian mitochondria is considered essential for replication, transcription, and translation of the mitochondrial genome but the pathway(s) and factors that control this import are poorly understood. Previously, we localized polynucleotide phosphorylase (PNPASE), a 3' --> 5' exoribonuclease and poly-A polymerase, in the mitochondrial ...
Yavuz Oktay, Samuel W French, Carla M Koehler   +2 more
exaly   +6 more sources

CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of pnp Transcripts That Have Been Previously Processed by RNase III and PNPase [PDF]

Journal of Bacteriology, 2015
ABSTRACT Csr is a conserved global regulatory system that represses or activates gene expression posttranscriptionally. CsrA of Escherichia coli is a homodimeric RNA binding protein that regulates transcription elongation, translation initiation, and mRNA stability by binding to the 5′ untranslated leader ...
Hongmarn Park, Helen Yakhnin, Michael A. Connolly, Tony Romeo, Paul Babitzke   +4 more
semanticscholar   +4 more sources

Crystal structure of dimeric human PNPase reveals why disease-linked mutants suffer from low RNA import and degradation activities [PDF]

Nucleic Acids Research, 2018
Human polynucleotide phosphorylase (PNPase) is an evolutionarily conserved 3′-to-5′ exoribonuclease principally located in mitochondria where it is responsible for RNA turnover and import.
Bagher Golzarroshan, Chia-Liang Lin, Hanna S Yuan   +2 more
exaly   +3 more sources