Abstract:
: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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Stanislauskienė R,Laurynėnas A,Rutkienė R,Aučynaitė A,Tauraitė D,Meškienė R,Urbelienė N,Kaupinis A,Valius M,Kaliniene L,Meškys Rdoi
10.1038/s41598-020-57664-wsubject
Has Abstractpub_date
2020-01-21 00:00:00pages
788issue
1issn
2045-2322pii
10.1038/s41598-020-57664-wjournal_volume
10pub_type
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