Identification of a stable complex between a [NiFe]‐hydrogenase catalytic subunit and its maturation protease

Marta Albareda, Grant Buchanan, Frank Sargent (Lead / Corresponding author)

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Abstract

Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory electron donor. This is facilitated by three [NiFe]‐hydrogenases termed Hyd‐1, Hyd‐2 and Hyd‐5. Hyd‐1 and Hyd‐5 are homologous oxygen‐tolerant [NiFe]‐hydrogenases. A critical step in the biosynthesis of a [NiFe]‐hydrogenase is the proteolytic processing of the catalytic subunit. In this work, the role of the maturation protease encoded within the Hyd‐5 operon, HydD, was found to be partially complemented by the maturation protease encoded in the Hyd‐1 operon, HyaD. In addition, both maturation proteases were shown to form stable complexes, in vivo and in vitro, with the catalytic subunit of Hyd‐5. The protein‐protein interactions were not detectable in a strain that could not make the enzyme metallocofactor.  
Original languageEnglish
Pages (from-to)338-347
Number of pages10
JournalFEBS Letters
Volume591
Issue number2
Early online date28 Dec 2016
DOIs
Publication statusPublished - Jan 2017

Keywords

  • Salmonella enterica
  • anaerobic respiration
  • bacterial hydrogen metabolism
  • metalloenzyme biosynthesis
  • [NiFe]‐hydrogenase
  • protein‐protein interactions

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