Respiratory protein interactions in Dehalobacter sp. strain 8M revealed through genomic and native proteomic analyses
Soder-Walz, Jesica M. (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Wasmund, Kenneth (University of Vienna)
Deobald, Darja (Helmholtz Centre for Environmental Research)
Vicent i Huguet, Teresa (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)
Adrian, Lorenz (Technische Universität Berlin)
Marco Urrea, Ernest (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental)

Data:	2023
Resum:	Dehalobacter (Firmicutes) encompass obligate organohalide-respiring bacteria used for bioremediation of groundwater contaminated with halogenated organics. Various aspects of their biochemistry remain unknown, including the identities and interactions of respiratory proteins. Here, we sequenced the genome of Dehalobacter sp. strain 8M and analysed its protein expression. Strain 8M encodes 22 reductive dehalogenase homologous (RdhA) proteins. RdhA D8M_v2_40029 (TmrA) was among the two most abundant proteins during growth with trichloromethane and 1,1,2-trichloroethane. To examine interactions of respiratory proteins, we used blue native gel electrophoresis together with dehalogenation activity tests and mass spectrometry. The highest activities were found in gel slices with the highest abundance of TmrA. Protein distributions across gel lanes provided biochemical evidence that the large and small subunits of the membrane-bound [NiFe] uptake hydrogenase (HupL and HupS) interacted strongly and that HupL/S interacted weakly with RdhA. Moreover, the interaction of RdhB and membrane-bound b-type cytochrome HupC was detected. RdhC proteins, often encoded in rdh operons but without described function, migrated in a protein complex not associated with HupL/S or RdhA. This study provides the first biochemical evidence of respiratory protein interactions in Dehalobacter, discusses implications for the respiratory architecture and advances the molecular comprehension of this unique respiratory chain.
Ajuts:	Agencia Estatal de Investigación PID2019-103989RB-I00 Agència de Gestió d'Ajuts Universitaris i de Recerca 2021/SGR-01008
Drets:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Publicat a:	Environmental Microbiology, (July 2023) , p. 1-17, ISSN 1462-2920

DOI: 10.1111/1462-2920.16464
PMID: 37452527

17 p, 4.4 MB

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