Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds

<p>Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown <em>Escherichia coli</em> to synthesise the holo forms of either its endogenous <em>c</em>-type cytochrome nitrite red...

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Main Authors: Sambongi, Y, Ferguson, S
Other Authors: Federation of European Biochemical Societies
Format: Journal article
Language:English
Published: Elsevier 1996
Subjects:
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author Sambongi, Y
Ferguson, S
author2 Federation of European Biochemical Societies
author_facet Federation of European Biochemical Societies
Sambongi, Y
Ferguson, S
author_sort Sambongi, Y
collection OXFORD
description <p>Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown <em>Escherichia coli</em> to synthesise the holo forms of either its endogenous <em>c</em>-type cytochrome nitrite reductase or exogenous cytochrome <em>c</em><sub>550</sub> from <em>Paracoccus denitrificans</em>. The synthesis of both cytochromes can be restored to the mutants by inclusion in the growth media of compounds containing disulphide bonds, e.g., the oxidised form of glutathione. The results suggest that the attachment of haem to the CXXCH motif of a periplasmic <em>c</em>-type cytochrome may be preceded by the formation of one or more intra- or intermolecular disulphide bonds involving the cysteine residues of this motif.</p>
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spelling oxford-uuid:883ec577-69be-436a-845b-cce794a6e5932022-03-26T22:15:57ZMutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compoundsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:883ec577-69be-436a-845b-cce794a6e593BiochemistryEnglishOxford University Research Archive - ValetElsevier1996Sambongi, YFerguson, SFederation of European Biochemical Societies<p>Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown <em>Escherichia coli</em> to synthesise the holo forms of either its endogenous <em>c</em>-type cytochrome nitrite reductase or exogenous cytochrome <em>c</em><sub>550</sub> from <em>Paracoccus denitrificans</em>. The synthesis of both cytochromes can be restored to the mutants by inclusion in the growth media of compounds containing disulphide bonds, e.g., the oxidised form of glutathione. The results suggest that the attachment of haem to the CXXCH motif of a periplasmic <em>c</em>-type cytochrome may be preceded by the formation of one or more intra- or intermolecular disulphide bonds involving the cysteine residues of this motif.</p>
spellingShingle Biochemistry
Sambongi, Y
Ferguson, S
Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title_full Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title_fullStr Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title_full_unstemmed Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title_short Mutants of Escherichia coli lacking disulphide oxdoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds
title_sort mutants of escherichia coli lacking disulphide oxdoreductases dsba and dsbb cannot synthesise an exogenous monohaem c type cytochrome except in the presence of disulphide compounds
topic Biochemistry
work_keys_str_mv AT sambongiy mutantsofescherichiacolilackingdisulphideoxdoreductasesdsbaanddsbbcannotsynthesiseanexogenousmonohaemctypecytochromeexceptinthepresenceofdisulphidecompounds
AT fergusons mutantsofescherichiacolilackingdisulphideoxdoreductasesdsbaanddsbbcannotsynthesiseanexogenousmonohaemctypecytochromeexceptinthepresenceofdisulphidecompounds