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Merck
CN

N9914

Sigma-Aldrich

Polynucleotide phosphorylase from Synechocystis sp.

recombinant, expressed in E. coli

别名:

PNPase, Polyribonucleotide Nucleotidyltransferase

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About This Item

MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54

生物来源

bacterial (Synechocystis sp.)

质量水平

重组

expressed in E. coli

描述

Histidine tagged

检测方案

90% (SDS-PAGE)

形式

solution

比活

≥500 units/mg protein

分子量

85 kDa

技术

cell based assay: suitable

适用性

suitable for molecular biology

应用

cell analysis

运输

dry ice

储存温度

−70°C

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一般描述

Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase.

应用

Polynucleotide phosphorylase has been used in a study to discover that a major function of PNPase is the synthesis of CDP. It has also been used in a study to investigate the enzyme responsible for RNA 3′-tail synthesis in S. coelicolor.

生化/生理作用

Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity.
Polynucleotide phosphorylase localizes to the intermembrane space of mitochondria and has a critical function in regulating mitochondrial homeostasis in human cells.

单位定义

One unit will polymerize 1.0 μmole of ADP, releasing 1.0 μmole of inorganic phosphate in 15 minutes, at pH 9.1 at 37 °C.
Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 60 mM KCl, 20% (w/v) Glycerol

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品

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Ruth Rott et al.
The Journal of biological chemistry, 278(18), 15771-15777 (2003-02-26)
The mechanism of RNA degradation in Escherichia coli involves endonucleolytic cleavage, polyadenylation of the cleavage product by poly(A) polymerase, and exonucleolytic degradation by the exoribonucleases, polynucleotide phosphorylase (PNPase) and RNase II. The poly(A) tails are homogenous, containing only adenosines in
G G Liou et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(1), 63-68 (2001-01-03)
RNase E isolated from Escherichia coli is contained in a multicomponent "degradosome" complex with other proteins implicated in RNA decay. Earlier work has shown that the C-terminal region of RNase E is a scaffold for the binding of degradosome components
A Danchin
DNA research : an international journal for rapid publication of reports on genes and genomes, 4(1), 9-18 (1997-02-28)
Genome comparison permits identification of chromosome regions conserved during evolution. Bacillus subtilis and Escherichia coli are so distant that there exists very few conserved landmarks in their genome organisation. Analysis of the conserved cmk rpsA cluster pinpointed the importance of
Patricia Bralley et al.
Microbiology (Reading, England), 152(Pt 3), 627-636 (2006-03-04)
As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for
Elinne Becket et al.
Journal of bacteriology, 194(20), 5613-5620 (2012-08-21)
Polynucleotide phosphorylase (PNP) plays a central role in RNA degradation, generating a pool of ribonucleoside diphosphates (rNDPs) that can be converted to deoxyribonucleoside diphosphates (dNDPs) by ribonucleotide reductase. We report here that spontaneous mutations resulting from replication errors, which are

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