luxA Gene From Enhygromyxa salina Encodes a Functional Homodimeric Luciferase

Author:

Yudenko Anna1,Bazhenov Sergey V.1,Aleksenko Vladimir A.1,Goncharov Ivan M.1,Semenov Oleg1,Remeeva Alina1,Nazarenko Vera V.1,Kuznetsova Elizaveta1,Fomin Vadim V.1,Konopleva Maria N.1,Al Ebrahim Rahaf1,Sluchanko Nikolai N.2,Ryzhykau Yury13,Semenov Yury S.1,Kuklin Alexander13,Manukhov Ilya V.1,Gushchin Ivan1ORCID

Affiliation:

1. Research Center for Molecular Mechanisms of Aging and Age‐Related Diseases Moscow Institute of Physics and Technology Dolgoprudny Russia

2. A.N. Bach Institute of Biochemistry Federal Research Center of Biotechnology of the Russian Academy of Sciences Moscow Russia

3. Frank Laboratory of Neutron Physics Joint Institute for Nuclear Research Dubna Russia

Abstract

ABSTRACTSeveral 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, EsLuxA is much less bright compared with luciferases from Aliivibrio fischeri (AfLuxAB) and Photorhabdus luminescens (PlLuxAB), and most active with medium‐chain C4–C9 aldehydes. Crystal structure of EsLuxA 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 EsLuxA. Phylogenetic analysis shows EsLuxA 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.

Funder

Russian Science Foundation

Ministry of Science and Higher Education of the Russian Federation

Publisher

Wiley

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