Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments

The formic acid extracts of several glutathione-deficient strains of Escherichia coli have been assayed for the presence of the mixed disulfide of CoA and glutathione, CoASSG. Strains deficient in γ-glutamyl-cysteine synthase (EC 6.3.2.2) produced only CoA dimer. Strains deficient in glutathione synthase (EC 6.3.2.3) produced the mixed disulfide of CoA and the γ-glutamyl-cysteine dipeptide. The pool size of total CoA in the cell did not change significantly even in the absence of glutathione.

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NMR Assignments, Secondary Structure and Hydration of Oxidized Escherichia coli Flavodoxin

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1997.00384.x ◽

1997 ◽

Vol 244 (2) ◽

pp. 384-399 ◽

Cited By ~ 8

Author(s):

Hannes Ponstingl ◽

Gottfried Otting

Keyword(s):

Escherichia Coli ◽

Secondary Structure ◽

Nmr Assignments

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The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione

Journal of Molecular Biology ◽

10.1006/jmbi.1994.1108 ◽

1994 ◽

Vol 235 (5) ◽

pp. 1585-1597 ◽

Cited By ~ 99

Author(s):

John H. Bushweller ◽

Martin Billeter ◽

Arne Holmgren ◽

Kurt Wüthrich

Keyword(s):

Escherichia Coli ◽

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Solution Structure ◽

Mixed Disulfide ◽

Resonance Solution ◽

Nuclear Magnetic

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Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1992.tb16616.x ◽

1992 ◽

Vol 204 (1) ◽

pp. 137-146 ◽

Cited By ~ 8

Author(s):

Katherine L. B. BORDEN ◽

Christopher J. BAUER ◽

Thomas A. FRENKIEL ◽

Pamela BECKMANN ◽

Andrew N. LANE

Keyword(s):

Escherichia Coli ◽

Nmr Assignments ◽

Three Dimensional ◽

Trp Repressor

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Sequence-specific proton NMR assignments and secondary structure in solution of Escherichia coli trp repressor

Biochemistry ◽

10.1021/bi00479a002 ◽

1990 ◽

Vol 29 (27) ◽

pp. 6332-6341 ◽

Cited By ~ 77

Author(s):

Cheryl H. Arrowsmith ◽

R. Pachter ◽

R. B. Altman ◽

S. B. Iyer ◽

O. Jardetzky

Keyword(s):

Escherichia Coli ◽

Secondary Structure ◽

Nmr Assignments ◽

Proton Nmr ◽

Trp Repressor ◽

Structure In Solution

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Partial characterization of the mode of inhibition of Escherichia coli RNA polymerase by the mixed disulfide, CoASSG

Canadian Journal of Biochemistry ◽

10.1139/o79-043 ◽

1979 ◽

Vol 57 (4) ◽

pp. 336-345 ◽

Cited By ~ 7

Author(s):

William C. H. Bees ◽

Peter C. Loewen

Keyword(s):

Escherichia Coli ◽

Rna Polymerase ◽

Equilibrium Dialysis ◽

Mixed Disulfide ◽

Nucleoside Triphosphates ◽

Noncompetitive Inhibitor ◽

Fe Complex ◽

Short Time ◽

Dna Template

The coenzyme A – glutathione mixed disulfide (CoASSG), when complexed with iron, is capable of inhibiting the RNA polymerase of Escherichia coli. A modified procedure involving a short time of exposure to high salt allowed the reliable preparation of CoASSG–Fe which was active in inhibiting RNA polymerase. The CoASSG–Fe complex acted as a noncompetitive inhibitor for the incorporation of all four nucleoside triphosphates but had a greater effect on GMP and CMP incorporation than AMP and UMP incorporation. Neither temperature nor ionic-strength changes affected CoASSG–Fe inhibition, and the use of rifampicin showed that CoASSG–Fe did not inhibit either the initiation or elongation processes of the polymerase. CoASSG–Fe was a more effective inhibitor at low DNA-template concentrations and it was more effective in inhibiting the incorporation of CMP and GMP on simple dG-dC containing templates and the asymmetric polymer poly d(T-C)∙poly d(G-A). The inhibition of transcription of poly d(I-C) was less effective than the inhibition of transcription of poly d(G-C). Equilibrium dialysis in microdialysis cells showed that CoASSG–Fe could associate with DNA in the absence of RNA polymerase.

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