Title YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N 4-acylcytosine derivatives /
Authors Stanislauskienė, Rūta ; Laurynėnas, Audrius ; Rutkienė, Rasa ; Aučynaitė, Agota ; Tauraitė, Daiva ; Meškienė, Rita ; Urbelienė, Nina ; Kaupinis, Algirdas ; Valius, Mindaugas ; Kalinienė, Laura ; Meškys, Rolandas
DOI 10.1038/s41598-020-57664-w
Full Text Download
Is Part of Scientific reports.. London : Nature Publishing Group. 2020, vol. 10, no. 1, p. 5203-5211.. eISSN 2045-2322
Abstract [eng] Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid Escherichia coli protein YqfB, previously identified as hypothetical, is a unique ASCH domain-containing amidohydrolase responsible for the catabolism of N4-acetylcytidine (ac4C). YqfB has several interesting and unique features: i) it is the smallest monomeric amidohydrolase described to date, ii) it is active towards structurally different N4-acylated cytosines/cytidines, and iii) it has a high specificity for these substrates (kcat/Km up to 2.8 × 106 M−1 s−1). Moreover, our results suggest that YqfB contains a unique Thr-Lys-Glu catalytic triad, and Arg acting as an oxyanion hole. The mutant lacking the yqfB gene retains the ability to grow, albeit poorly, on N4-acetylcytosine as a source of uracil, suggesting that an alternative route for the utilization of this compound exists in E. coli. Overall, YqfB ability to hydrolyse various N4-acylated cytosines and cytidines not only sheds light on the long-standing mystery of how ac4C is catabolized in bacteria, but also expands our knowledge of the structural diversity within the active sites of amidohydrolases.
Published London : Nature Publishing Group
Type Journal article
Language English
Publication date 2020
CC license CC license description