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Activation of a [nife]-hydrogenase-4 isoenzyme by maturation proteases

Lookup NU author(s): Dr Alexander FinneyORCiD, Dr Grant Buchanan, Professor Tracy Palmer FRS FRSE FMedSciORCiD, Professor Frank SargentORCiD

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Abstract

© 2020 The Authors.Maturation of [NiFe]-hydrogenases often involves specific proteases responsible for cleavage of the catalytic subunits. Escherichia coli HycI is the protease dedicated to maturation of the Hydrogenase-3 isoenzyme, a component of formate hydrogenlyase-1. In this work, it is demonstrated that a Pectobacterium atrosepticum HycI homologue, HyfK, is required for hydrogenase-4 activity, a component of formate hydrogenlyase-2, in that bacterium. The P. atrosepticum ΔhyfK mutant phenotype could be rescued by either P. atrosepticum hyfK or E. coli hycI on a plasmid. Conversely, an E. coli ΔhycI mutant was complemented by either E. coli hycI or P. atrosepticum hyfK in trans. E. coli is a rare example of a bacterium containing both hydrogenase-3 and hydrogenase-4, however the operon encoding hydrogenase-4 has no maturation protease gene. This work suggests HycI should be sufficient for maturation of both E. coli formate hydrogenlyases, however no formate hydrogenlyase-2 activity was detected in any E. coli strains tested here.

Publication metadata

Author(s): Finney AJ, Buchanan G, Palmer T, Coulthurst SJ, Sargent F

Publication type: Article

Publication status: Published

Journal: Microbiology

Year: 2020

Volume: 166

Issue: 9

Pages: 854-860

Online publication date: 30/07/2020

Acceptance date: 22/07/2020

Date deposited: 16/11/2020

ISSN (print): 1350-0872

ISSN (electronic): 1465-2080

Publisher: Microbiology Society

URL: https://doi.org/10.1099/mic.0.000963

DOI: 10.1099/mic.0.000963

PubMed id: 32731905

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