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| Main Authors: | , , , , , , , , , , , , , , , , |
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| Format: | Artículo Open Access |
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Wiley
2024
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| Online Access: | https://onlinelibrary.wiley.com/doi/10.1002/prot.26739 |
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- luxA Gene From Enhygromyxa salina Encodes a Functional Homodimeric Luciferase Anna Yudenko Sergey V. Bazhenov Vladimir A. Aleksenko Ivan M. Goncharov Oleg Semenov Alina Remeeva Vera V. Nazarenko Elizaveta Kuznetsova Vadim V. Fomin Maria N. Konopleva Rahaf Al Ebrahim Nikolai N. Sluchanko Yury Ryzhykau Yury S. Semenov Alexander Kuklin Ilya V. Manukhov Ivan Gushchin Proteins: Structure, Function, and Bioinformatics ABSTRACT Several clades of luminescent bacteria are known currently. They all contain similar lux operons, which include the genes luxA and luxB encoding a heterodimeric luciferase. The aldehyde oxygenation reaction is presumed to be catalyzed primarily by the subunit LuxA, whereas LuxB is required for efficiency and stability of the complex. Recently, genomic analysis identified a subset of bacterial species with rearranged lux operons lacking luxB . Here, we show that the product of the luxA gene from the reduced luxACDE operon of Enhygromyxa salina is luminescent upon addition of aldehydes both in vivo in Escherichia coli and in vitro. Overall, Es LuxA is much less bright compared with luciferases from Aliivibrio fischeri ( Af LuxAB) and Photorhabdus luminescens ( Pl LuxAB), and most active with medium‐chain C4–C9 aldehydes. Crystal structure of Es LuxA determined at the resolution of 2.71 Å reveals a (β/α) 8 TIM‐barrel fold, characteristic for other bacterial luciferases, and the protein preferentially forms a dimer in solution. The mobile loop residues 264–293, which form a β‐hairpin or a coil in Vibrio harveyi LuxA, form α‐helices in Es LuxA. Phylogenetic analysis shows Es LuxA and related proteins may be bacterial protoluciferases that arose prior to duplication of the luxA gene and its speciation to luxA and luxB in the previously described luminescent bacteria. Our work paves the way for the development of new bacterial luciferases that have an advantage of being encoded by a single gene. 10.1002/prot.26739 http://onlinelibrary.wiley.com/termsAndConditions#vor