Biochemical, structural, and functional studies reveal that MAB_4324c from &lt;em&gt;Mycobacterium abscessus&lt;/em&gt; is an active tandem repeat &lt;em&gt;N&lt;/em&gt;‐acetyltransferase

Alsarraf, Husam M.A.B.; Ung, Kien Lam; Johansen, Matt D.; Dimon, Juliette; Olieric, Vincent; Kremer, Laurent; Blaise, Mickaël

doi:10.1002/1873-3468.14360

Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N‐acetyltransferase

Alsarraf HMAB, Ung KL, Johansen MD, Dimon J, Olieric V, Kremer L & Blaise M

Citation

Alsarraf, H. M. A. B., Ung, K. L., Johansen, M. D., Dimon, J., Olieric, V., Kremer, L., & Blaise, M. (2022). Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N‐acetyltransferase. FEBS Letters, 596(12), 1516-1532. https://doi.org/10.1002/1873-3468.14360

Persistent URL https://www.dora.lib4ri.ch/psi/islandora/object/psi:43173

Mycobacterium abscessus is a pathogenic non-tuberculous mycobacterium that possesses an intrinsic drug resistance profile. Several N-acetyltransferases mediate drug resistance and/or participate in M. abscessus virulence. Mining the M. abscessus genome has revealed genes encoding additional N-acetyltransferases whose functions remain uncharacterized, among them MAB_4324c. Here, we showed that the purified MAB_4324c protein is a N-acetyltransferase able to acetylate small polyamine substrates. The crystal structure of MAB_4324c was solved at high resolution in complex with its cofactor, revealing the presence of two GCN5-related N-acetyltransferase domains and a cryptic binding site for NADPH. Genetic studies demonstrate that MAB_4324c is not essential for in vitro growth of M. abscessus; however, overexpression of the protein enhanced the uptake and survival of M. abscessus in THP-1 macrophages.