Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase

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Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase.

Essential for DNA biosynthesis and repair, ribonucleotide reductases (RNRs) convert ribonucleotides to deoxyribonucleotides via radical-based chemistry. Although long known that allosteric regulation of RNR activity is vital for cell health, the molecular basis of this regulation has been enigmatic, largely due to a lack of structural information about how the catalytic subunit (α(2)) and the r...

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Ribonucleotide reductase (RNR) is an essential enzyme for all living organisms since is the responsible for the last step in the synthesis of the four deoxyribonucleotides (dNTPs) necessary for DNA replication and repair. In this work, we have investigated the expression of the three-RNR classes (Ia, Ib and III) during Escherichia coli biofilm formation. We show the temporal and spatial importa...

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The expression of the genes encoding ribonucleotide reductase in Escherichia coli was investigated in cultures synchronized by obtaining the smallest cells in a population after sucrose gradient centrifugation. Specific activity of ribonucleotide reductase and DNA initiation were found to increase in parallel, periodically as a function of the cell cycle. The expression of nrd was also determin...

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Importance of the Maintenance Pathway in the Regulation of the Activity of Escherichia coli Ribonucleotide Reductase†

Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides in all organisms. The Escherichia coli class Ia RNR is composed of alpha and beta subunits that form an alpha 2beta 2 active complex. beta contains the diferric tyrosyl radical (Y (*)) cofactor that is essential for the reduction process that occurs on alpha. [Y (*)] in vitro is proportional to RNR activ...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2011

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1112715108