Trading in cooperativity for specificity to maintain uracil-free DNA
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Tartalom: http://real.mtak.hu/37888/
Archívum: MTA Könyvtár
Gyűjtemény: Status = Published


Type = Article
Cím:
Trading in cooperativity for specificity to maintain uracil-free DNA
Létrehozó:
SzabĂł, Judit Eszter
Takacs, E.
Merenyi, G.
Vértessy G., Beáta
Toth, J.
Kiadó:
Nature Publishing Group
Dátum:
2016
Téma:
QH301 Biology / biolĂłgia
QH3011 Biochemistry / biokémia
Tartalmi leírás:
Members of the dUTPase superfamily play an important role in the maintenance of the pyrimidine nucleotide balance and of genome integrity. dCTP deaminases and the bifunctional dCTP deaminase-dUTPases are cooperatively regulated by dTTP. However, the manifestation of allosteric behavior within the same trimeric protein architecture of dUTPases, the third member of the superfamily, has been a question of debate for decades. Therefore, we designed hybrid dUTPase trimers to access conformational states potentially mimicking the ones observed in the cooperative relatives. We studied how the interruption of different steps of the enzyme cycle affects the active site cross talk. We found that subunits work independently in dUTPase. The experimental results combined with a comparative structural analysis of dUTPase superfamily enzymes revealed that subtile structural differences within the allosteric loop and the central channel in these enzymes give rise to their dramatically different cooperative behavior. We demonstrate that the lack of allosteric regulation in dUTPase is related to the functional adaptation to more efficient dUTP hydrolysis which is advantageous in uracil-DNA prevention.
Nyelv:
angol
Típus:
Article
PeerReviewed
info:eu-repo/semantics/article
Formátum:
text
Azonosító:
Szabó, Judit Eszter and Takacs, E. and Merenyi, G. and Vértessy G., Beáta and Toth, J. (2016) Trading in cooperativity for specificity to maintain uracil-free DNA. SCIENTIFIC REPORTS (6). No. 24219. ISSN 2045-2322
Kapcsolat:
MTMT:3052621; doi:10.1038/srep24219