Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: STRUCTURAL MAPPING AND EFFECT ON mRNA TURNOVER. [PDF]
J 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
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Localization of components of the RNA-degrading machine in Bacillus subtilis [PDF]
Frontiers 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
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Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase [PDF]
Nucleic 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.
C. Portier, A. Guissani
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Cell 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
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Distinctive effects of domain deletions on the manganese-dependent DNA polymerase and DNA phosphorylase activities of Mycobacterium smegmatis polynucleotide phosphorylase. [PDF]
Biochemistry, 2013 Unciuleac MC, Shuman S.
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region. [PDF]
RNA, 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
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STUDIES ON POLYNUCLEOTIDES SYNTHESIZED BY POLYNUCLEOTIDE PHOSPHORYLASE [PDF]
Journal of Biological Chemistry, 1957 Severo Ochoa +5 more
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Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly [PDF]
Open Biology, 2012 Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3′–5′ directionality and processive behaviour.
Steven W. Hardwick +4 more
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Helicase SUV3, polynucleotide phosphorylase, and mitochondrial polyadenylation polymerase form a transient complex to modulate mitochondrial mRNA polyadenylated tail lengths in response to energetic changes. [PDF]
J Biol Chem, 2014 Background: Helicase SUV3, polynucleotide phosphorylase (PNPase), or mitochondrial poly(A) polymerases (mtPAP) have individual activity in regulating mitochondrial mRNA (mt-mRNA)-polyadenylated (poly(A)) tails.
Wang DD +5 more
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Exploring the mitochondrial microRNA import pathway through Polynucleotide Phosphorylase (PNPase). [PDF]
J Mol Cell Cardiol, 2017 Shepherd DL +9 more
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