Results 201 to 210 of about 4,071 (219)
RNase R vs. PNPase: selecting the best-suited exoribonuclease for environmental adaptation
Extremophiles3' → 5' exoribonucleases play a critical role in many aspects of RNA metabolism. RNase R, PNPase, and RNase II are the major contributors to RNA processing, maturation, and quality control in bacteria. Bacteria don't seem to have dedicated RNA degradation machineries to process different classes of RNAs.
Theetha L Pavankumar
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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 +4 more sources
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 +4 more sources
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
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
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.
Shawn M.D. Bearson +3 more
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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.
Shawn M.D. Bearson +3 more
openaire +3 more sources
Modular domain organization of RNase E and PNPase
2002mRNA 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.
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Phenotypic characterization of PNPase knockdown in C. elegans
2015VCU Theses and ...
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PNPase IN C. ELEGANS: MUTAGENIC ANALYSIS TO COMPLEMENT KNOCKDOWN STUDIES
2017VCU Theses and ...
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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
Cecília M. Arraiano +3 more
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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
Cecília M. Arraiano +3 more
openaire +3 more sources