Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor

Szirák, Krisztina; Keserű, Judit; Bíró, Sándor; Schmelczer, Iván; Barabás, György; Penyige, András

doi:10.1007/s12275-012-1440-y

Cited by 10 publications

(14 citation statements)

References 30 publications

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“…Scattered evidence suggests that ADP-ribosylation in bacteria is much more common in regulating important cellular pathways, e.g. development and possibly mediating cell-cell contact in M. xanthus (18, 19), differentiation process in B. subtilis (21), and differentiation and secondary metabolism in Streptomyces (22, 37). Finally, here we suggest the possible involvement of the de-ADP-ribosylation process in the control of S. coelicolor antibiotic production.…”

Section: Discussionmentioning

confidence: 99%

“…In accordance with structural similarity with two toxic ADP-ribosyltransferases, pierisins and mosquitocidal toxin, SCO5461 has been described as a DNA-modifying exotoxin, and its ADP-ribosylating activity toward N2 amino groups of guanine nucleosides, as well as mononucleotides, has been shown (28). Szirák et al (37) have shown that disruption of SCO5461 leads to conditional pleiotropic phenotype characterized by morphological differentiation and antibiotic production defects. In addition, the same authors showed that deficiency in SCO5461 leads to a minor effect in protein ADP-ribosylation patterns; however, the question remained whether the effect was direct (37).…”

Section: Discussionmentioning

confidence: 99%

“…Szirák et al (37) have shown that disruption of SCO5461 leads to conditional pleiotropic phenotype characterized by morphological differentiation and antibiotic production defects. In addition, the same authors showed that deficiency in SCO5461 leads to a minor effect in protein ADP-ribosylation patterns; however, the question remained whether the effect was direct (37). Here we confirmed auto mono-ADP-ribosylating activity of the SCO5461 protein in vitro , but its specific protein trans targets are yet to be discovered.…”

Section: Discussionmentioning

confidence: 99%

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Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Lalić¹,

Marjanović²,

Palazzo

et al. 2016

Journal of Biological Chemistry

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ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that bind ADP-ribose derivatives and are found in proteins with diverse cellular functions. Some proteins from the macrodomain family can hydrolyze ADP-ribosylated substrates and therefore reverse this post-translational modification. Bacteria and Streptomyces, in particular, are known to utilize protein ADP-ribosylation, yet very little is known about their enzymes that synthesize and remove this modification. We have determined the crystal structure and characterized, both biochemically and functionally, the macrodomain protein SCO6735 from Streptomyces coelicolor. This protein is a member of an uncharacterized subfamily of macrodomain proteins. Its crystal structure revealed a highly conserved macrodomain fold. We showed that SCO6735 possesses the ability to hydrolyze PARP-dependent protein ADP-ribosylation. Furthermore, we showed that expression of this protein is induced upon DNA damage and that deletion of this protein in S. coelicolor increases antibiotic production. Our results provide the first insights into the molecular basis of its action and impact on Streptomyces metabolism.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Lalić¹,

Marjanović²,

Palazzo

et al. 2016

Journal of Biological Chemistry

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“…SCO5461 orthologues are distributed in many Streptomyces spp. strains and Streptosporangium roseum, and an imperfect ORF remains in Streptomyces avermitilis (Szirák et al 2012;Nakano et al 2013). Contrary to pierisins, MTX, and Plx1, which shows toxicity (Shiga et al 2006;Thanabalu et al 1991;Schirmer et al 2002;Fünfhaus et al 2013), physiological roles for SCO5461 might not be toxin due to the lack of receptor-binding domains.…”

Section: Homologues Of the Pierisins And Carp-1mentioning

confidence: 99%

“…Contrary to pierisins, MTX, and Plx1, which shows toxicity (Shiga et al 2006;Thanabalu et al 1991;Schirmer et al 2002;Fünfhaus et al 2013), physiological roles for SCO5461 might not be toxin due to the lack of receptor-binding domains. Szirák et al (2012) have reported the possible ADP-ribosylation of a 65-kDa endogenous protein by SCO5461, and that a disruption of the SCO5461 gene affects sporulation and antibiotic production depending on the culture conditions. This deficiency is rescued by co-cultivation with a wild-type strain (Szirák et al 2012).…”

Section: Homologues Of the Pierisins And Carp-1mentioning

confidence: 99%

Endogenous ADP-Ribosylation

Koch‐Nolte¹

2015

Current Topics in Microbiology and Immunology

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Pierisins and CARP-1: ADP-Ribosylation of DNA by ARTCs in Butterflies and Shellfish

Nakano

Takahashi‐Nakaguchi

Yamamoto

et al. 2014

Endogenous ADP-Ribosylation

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The cabbage butterfly, Pieris rapae, and related species possess a previously unknown ADP-ribosylating toxin, guanine specific ADP-ribosyltransferase. This enzyme toxin, known as pierisin, consists of enzymatic N-terminal domain and receptor-binding C-terminal domain, or typical AB-toxin structure. Pierisin efficiently transfers an ADP-ribosyl moiety to the N(2) position of the guanine base of dsDNA. Receptors for pierisin are suggested to be the neutral glycosphingolipids, globotriaosylceramide (Gb3), and globotetraosylceramide (Gb4). This DNA-modifying toxin exhibits strong cytotoxicity and induces apoptosis in various human cell lines, which can be blocked by Bcl-2. Pierisin also produces detrimental effects on the eggs and larvae of the non-habitual parasitoids. In contrast, a natural parasitoid of the cabbage butterfly, Cotesia glomerata, was resistant to this toxin. The physiological role of pierisin in the butterfly is suggested to be a defense factor against parasitization by wasps. Other type of DNA ADP-ribosyltransferase is present in certain kinds of edible clams. For example, the CARP-1 protein found in Meretrix lamarckii consists of an enzymatic domain without a possible receptor-binding domain. Pierisin and CARP-1 are almost fully non-homologous at the amino acid sequence level, but other ADP-ribosyltransferases homologous to pierisin are present in different biological species such as eubacterium Streptomyces. Possible diverse physiological roles of the DNA ADP-ribosyltransferases are discussed.

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Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor

Cited by 10 publications

References 30 publications

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor

Endogenous ADP-Ribosylation

Pierisins and CARP-1: ADP-Ribosylation of DNA by ARTCs in Butterflies and Shellfish

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