Your browser doesn't support javascript.
loading
Bacteriophage T5 dUTPase: Combination of Common Enzymatic and Novel Functions.
Glukhov, Anatoly; Marchenkov, Victor; Dzhus, Ulyana; Krutilina, Antonina; Selikhanov, Georgii; Gabdulkhakov, Azat.
Afiliação
  • Glukhov A; Institute of Protein Research RAS, 142290 Pushchino, Russia.
  • Marchenkov V; Institute of Protein Research RAS, 142290 Pushchino, Russia.
  • Dzhus U; Institute of Protein Research RAS, 142290 Pushchino, Russia.
  • Krutilina A; Institute of Protein Research RAS, 142290 Pushchino, Russia.
  • Selikhanov G; Institute of Protein Research RAS, 142290 Pushchino, Russia.
  • Gabdulkhakov A; International Institute "Solution Chemistry of Advanced Materials and Technologies", ITMO University, 191002 St. Petersburg, Russia.
Int J Mol Sci ; 25(2)2024 Jan 10.
Article em En | MEDLINE | ID: mdl-38255966
ABSTRACT
The main function of dUTPases is to regulate the cellular levels of dUTP and dTTP, thereby playing a crucial role in DNA repair mechanisms. Despite the fact that mutant organisms with obliterated dUTPase enzymatic activity remain viable, it is not possible to completely knock out the dut gene due to the lethal consequences of such a mutation for the organism. As a result, it is considered that this class of enzymes performs an additional function that is essential for the organism's survival. In this study, we provide evidence that the dUTPase of bacteriophage T5 fulfills a supplemental function, in addition to its canonical role. We determined the crystal structure of bacteriophage T5 dUTPase with a resolution of 2.0 Å, and we discovered a distinct short loop consisting of six amino acid residues, representing a unique structural feature specific to the T5-like phages dUTPases. The removal of this element did not affect the overall structure of the homotrimer, but it had significant effects on the development of the phage. Furthermore, it was shown that the enzymatic function and the novel function of the bacteriophage T5 dUTPase are unrelated and independent from each other.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pirofosfatases / Bacteriófagos / Aminoácidos Idioma: En Revista: Int J Mol Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Federação Russa

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pirofosfatases / Bacteriófagos / Aminoácidos Idioma: En Revista: Int J Mol Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Federação Russa