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The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis in <i>Streptomyces</i>

Petrus, Marloes LC and Vijgenboom, Erik and Chaplin, Amanda K and Worrall, Jonathan AR and van Wezel, Gilles P and Claessen, Dennis (2016) 'The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis in <i>Streptomyces</i>.' Open Biology, 6 (1). p. 150149. ISSN 2046-2441

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<jats:p> The filamentous bacterium <jats:italic>Streptomyces lividans</jats:italic> depends on the radical copper oxidase GlxA for the formation of reproductive aerial structures and, in liquid environments, for the formation of pellets. Incorporation of copper into the active site is essential for the formation of a cross-linked tyrosyl-cysteine cofactor, which is needed for enzymatic activity. In this study, we show a crucial link between GlxA maturation and a group of copper-related proteins including the chaperone Sco and a novel DyP-type peroxidase hereinafter called DtpA. Under copper-limiting conditions, the <jats:italic>sco</jats:italic> and <jats:italic>dtpA</jats:italic> deletion mutants are blocked in aerial growth and pellet formation, similarly to a <jats:italic>glxA</jats:italic> mutant. Western blot analysis showed that GlxA maturation is perturbed in the <jats:italic>sco</jats:italic> and <jats:italic>dtpA</jats:italic> mutants, but both maturation and morphology can by rescued by increasing the bioavailability of copper. DtpA acts as a peroxidase in the presence of GlxA and is a substrate for the twin-arginine translocation (Tat) translocation pathway. In agreement, the maturation status of GlxA is also perturbed in <jats:italic>tat</jats:italic> mutants, which can be compensated for by the addition of copper, thereby partially restoring their morphological defects. Our data support a model wherein a copper-trafficking pathway and Tat-dependent secretion of DtpA link to the GlxA-dependent morphogenesis pathway. </jats:p>

Item Type: Article
Uncontrolled Keywords: morphogenesis; twin-arginine translocation; DyP-type peroxidase; cuproenzyme; GlxA maturation; glycan
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health
Faculty of Science and Health > Life Sciences, School of
SWORD Depositor: Elements
Depositing User: Elements
Date Deposited: 26 Feb 2016 21:04
Last Modified: 18 Aug 2022 11:07

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