The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years
RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzym...
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| Format: | Article |
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Portland Press
2012
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| Online Access: | http://hdl.handle.net/1721.1/73962 https://orcid.org/0000-0001-5486-2755 |
| _version_ | 1826210547843989504 |
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| author | Ando, Nozomi Zimanyi, Christina Marie Brignole, Edward J Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Ando, Nozomi Zimanyi, Christina Marie Brignole, Edward J Drennan, Catherine L |
| author_sort | Ando, Nozomi |
| collection | MIT |
| description | RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: β2 houses the diferric-tyrosyl radical cofactor, and α2 contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years. |
| first_indexed | 2024-09-23T14:51:24Z |
| format | Article |
| id | mit-1721.1/73962 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:51:24Z |
| publishDate | 2012 |
| publisher | Portland Press |
| record_format | dspace |
| spelling | mit-1721.1/739622022-10-01T22:57:43Z The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years Ando, Nozomi Zimanyi, Christina Marie Brignole, Edward J Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Drennan, Catherine L. Drennan, Catherine L. Brignole, Edward J. Ando, Nozomi Zimanyi, Christina Marie RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: β2 houses the diferric-tyrosyl radical cofactor, and α2 contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years. National Institutes of Health (U.S.) (T32GM08334) Howard Hughes Medical Institute (Investigator) National Institutes of Health (U.S.) (F32GM904862) National Institutes of Health (U.S.) (K99GM100008) National Institutes of Health (U.S.) (F32DK080622) National Institutes of Health (U.S.) (P30-ES002109) 2012-10-15T15:24:54Z 2012-10-15T15:24:54Z 2012-06 2012-03 Article http://purl.org/eprint/type/JournalArticle 0300-5127 1470-8752 http://hdl.handle.net/1721.1/73962 Brignole, Edward J. et al. “The Prototypic Class Ia Ribonucleotide Reductase from Escherichia Coli: Still Surprising After All These Years.” Biochemical Society Transactions 40.3 (2012): 523–530. Web. https://orcid.org/0000-0001-5486-2755 en_US http://dx.doi.org/10.1042/BST20120081 Biochemical Society Transactions Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Portland Press Edward Brignole |
| spellingShingle | Ando, Nozomi Zimanyi, Christina Marie Brignole, Edward J Drennan, Catherine L The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title | The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title_full | The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title_fullStr | The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title_full_unstemmed | The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title_short | The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years |
| title_sort | prototypic class ia ribonucleotide reductase from escherichia coli still surprising after all these years |
| url | http://hdl.handle.net/1721.1/73962 https://orcid.org/0000-0001-5486-2755 |
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