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- Hofer, AndersUmeå universitet,Institutionen för medicinsk kemi och biofysik (author)
DNA building blocks : keeping control of manufacture
- Article/chapterEnglish2012
Publisher, publication year, extent ...
- 2011-11-03
- London :Informa UK Limited,2012
- printrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:su-85272
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-85272URI
- https://doi.org/10.3109/10409238.2011.630372DOI
- https://lup.lub.lu.se/record/2333840URI
- https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-50091URI
Supplementary language notes
- Language:English
- Summary in:English
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Notes
- Ribonucleotide reductase (RNR) is the only source for de novo production of the four deoxyribonucleoside triphosphate (dNTP) building blocks needed for DNA synthesis and repair. It is crucial that these dNTP pools are carefully balanced, since mutation rates increase when dNTP levels are either unbalanced or elevated. RNR is the major player in this homeostasis, and with its four different substrates, four different allosteric effectors and two different effector binding sites, it has one of the most sophisticated allosteric regulations known today. In the past few years, the structures of RNRs from several bacteria, yeast and man have been determined in the presence of allosteric effectors and substrates, revealing new information about the mechanisms behind the allosteric regulation. A common theme for all studied RNRs is a flexible loop that mediates modulatory effects from the allosteric specificity site (s-site) to the catalytic site for discrimination between the four substrates. Much less is known about the allosteric activity site (a-site), which functions as an on-off switch for the enzyme's overall activity by binding ATP (activator) or dATP (inhibitor). The two nucleotides induce formation of different enzyme oligomers, and a recent structure of a dATP-inhibited α(6)β(2) complex from yeast suggested how its subunits interacted non-productively. Interestingly, the oligomers formed and the details of their allosteric regulation differ between eukaryotes and Escherichia coli. Nevertheless, these differences serve a common purpose in an essential enzyme whose allosteric regulation might date back to the era when the molecular mechanisms behind the central dogma evolved.
Subject headings and genre
- NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
- NATURVETENSKAP Biologi hsv//swe
- NATURAL SCIENCES Biological Sciences hsv//eng
- Ribonucleotide reductase
- RNR
- allosteric regulation
- specificity site
- activity site
- ATP cone
- dATP inhibition
- Molecular Biology
- molekylärbiologi
- Ribonucleotide reductase
- RNR
- allosteric regulation
- specificity site
- activity site
- ATP cone
- dATP inhibition
Added entries (persons, corporate bodies, meetings, titles ...)
- Crona, MikaelStockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik(Swepub:su)micr1256 (author)
- Logan, DerekLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)mbfys-do (author)
- Sjöberg, Britt-MarieStockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik(Swepub:su)bsjob (author)
- Umeå universitetInstitutionen för medicinsk kemi och biofysik (creator_code:org_t)
Related titles
- In:Critical reviews in biochemistry and molecular biologyLondon : Informa UK Limited47:1, s. 50-631040-92381549-7798
Internet link
- https://doi.org/10.3109/10409238.2011.630372Fulltext
- https://europepmc.org/articles/pmc3267527?pdf=render
- http://dx.doi.org/10.3109/10409238.2011.630372FULLTEXT
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-85272
- https://doi.org/10.3109/10409238.2011.630372
- https://lup.lub.lu.se/record/2333840
- https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-50091
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