DNA building blocks: keeping control of manufacture

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DNA building blocks : keeping control of manufacture

Hofer, Anders (author): Umeå universitet,Institutionen för medicinsk kemi och biofysik

Crona, Mikael (author): Stockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik

Logan, Derek (author): Lund 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

Sjöberg, Britt-Marie (author): Stockholms universitet,Institutionen för molekylärbiologi och funktionsgenomik

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(creator_code:org_t)

2011-11-03
2012
English.
In: Critical reviews in biochemistry and molecular biology. - London : Informa UK Limited. - 1040-9238 .- 1549-7798. ; 47:1, s. 50-63

Related links:: https://doi.org/10.3...; show more...; https://europepmc.or...; http://dx.doi.org/10...; https://urn.kb.se/re...; https://doi.org/10.3...; https://lup.lub.lu.s...; https://urn.kb.se/re...; show less...

Research review (peer-reviewed)

Abstract Subject headings

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

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)

Keyword

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

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By the author/editor: Hofer, Anders; Crona, Mikael; Logan, Derek; Sjöberg, Britt-M ...

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NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Biochemistry and ...

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...

Articles in the publication: Critical reviews ...

By the university: Stockholm University; Lund University; Umeå University

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