Ribonucleoside diphosphate reductase is a component of the replication hyperstructure in Escherichia coli
نویسندگان
چکیده
منابع مشابه
Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli.
Ribonucleotide reductase from Escherichia coli consists of two nonidentical subunits, proteins Bl and B2. Affinity chromatography resulted in a Bl preparation which appeared homogeneous during polyacrylamide gel electrophoresis and ultracentrifugation. The molecular weight was 160,000 by sedimentation equilibrium centrifugation using a partial specific volume of 0.706 ml per g at 4”. Protein Bl...
متن کاملReaction Mechanism of Ribonucleoside Diphosphate Reductase from Escherichia coli
Ribonucleoside diphosphate reductase consists of two nonidentical subunits, proteins Bl and B2. The enzyme catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides. The electrons required in this reduction are transported from NADPH via a flavoprotein, thioredoxin reductase, to a low molecular weight protein, thioredoxin. The reduced form of thioredoxin acts as hydro...
متن کاملActive Site of Ribonucleoside Diphosphate Reductase from Escherichia coli
Ribonucleoside diphosphate reductase is an allosteric enzyme consisting of two nonidentical subunits, proteins Bl and B2. Bl contains dithiols which participate in the oxidation-reduction reactions of electron transport, while B2 contains a free radical essential for activity. Ribonucleoside diphosphates are bound to Bl but not to B2. Addition of 2’-deoxy-2’-chloro ribonucleoside diphosphates t...
متن کاملDefective ribonucleoside diphosphate reductase impairs replication fork progression in Escherichia coli.
The observed lengthening of the C period in the presence of a defective ribonucleoside diphosphate reductase has been assumed to be due solely to the low deoxyribonucleotide supply in the nrdA101 mutant strain. We show here that the nrdA101 mutation induces DNA double-strand breaks at the permissive temperature in a recB-deficient background, suggesting an increase in the number of stalled repl...
متن کاملActive site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2'-substituted ribonucleoside diphosphates.
Ribonucleoside diphosphate reductase is an allosteric enzyme consisting of two nonidentical subunits, proteins B1 and B2. B1 contains dithiols which participate in the oxidation-reduction reactions of electron transport, while B2 contains a free radical essential for activity. Ribonucleoside diphosphates are bound to B1 but not to B2. Addition of 2'-deoxy-2'-chloro ribonucleoside diphosphates t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2002
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.2002.02761.x