Mutational analysis of polynucleotide phosphorylase from Escherichia coli. (Q54540578)

31 May 2018

title

Mutational analysis of polynucleotide phosphorylase from Escherichia coli. (English)

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31 May 2018

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Anne Jarrige

1

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31 May 2018

Dominique Bréchemier-Baey

2

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31 May 2018

Nathalie Mathy

3

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31 May 2018

Ophélie Duché

4

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31 May 2018

Claude Portier

5

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31 May 2018

language of work or name

English

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publication date

1 August 2002

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31 May 2018

Journal of Molecular Biology

published in

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31 May 2018

volume

321

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31 May 2018

issue

3

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31 May 2018

page(s)

397-409

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31 May 2018

Kinetics of Polymerization and Phosphorolysis Reactions of Escherichia coli Polynucleotide Phosphorylase. Evidence for Multiple Binding of Polynucleotide in Phosphorolysis

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Kinetics of Polymerization and Phosphorolysis Reactions of E. coli Polynucleotide Phosphorylase. Role of Oligonucleotides in Polymerization

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Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts

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Polynucleotide phosphorylase functions both as a 3' right-arrow 5' exonuclease and a poly(A) polymerase in Escherichia coli

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The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein

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Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1.

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In vitro genetic analysis of the RNA binding site of vigilin, a multi-KH-domain protein

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The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold

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A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation

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Quaternary structure ofEscherichia colipolynucleotide phosphorylase: new evidence for a trimeric structure

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Quaternary Structure of Polynucleotide Phosphorylase from Escherichia coli: Evidence of a Complex between Two Types of Polypeptide Chains

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Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation

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Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase

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PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader

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Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation

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Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability

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A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli

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A point mutation in the FMR-1 gene associated with fragile X mental retardation

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Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome

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Increased expression of Escherichia coli polynucleotide phosphorylase at low temperatures is linked to a decrease in the efficiency of autocontrol

7 January 2021

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The first step in the functional inactivation of the Escherichia coli polynucleotide phosphorylase messenger is a ribonuclease III processing at the 5' end.

7 January 2021

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Isolation of a polynucleotide phosphorylase mutant using a kanamycin resistant determinant

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10.1016/S0022-2836(02)00645-9

7 January 2021

Identifiers

DOI

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31 May 2018

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31 May 2018