Self‐resistance of the nourseothricin‐producing strain <i>Streptomyces noursei</i>

Haupt, Ina; Thrum, H.; Noack, D.

doi:10.1002/jobm.3620260604

Cited by 9 publications

(3 citation statements)

References 16 publications

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“…Streptothricins are potent inhibitors of prokaryotic protein biosynthesis, but are not used therapeutically due to their nephrotoxicity [2]. Nourseothricin is currently being used under the name CloNat, and is an effective selective agent for molecular cloning technologies in fungi and plants [3–6]. On the other hand, streptothricins are also being tested as fungistatics in agriculture for the treatment of blast disease and other plant diseases [7].…”

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confidence: 99%

A β‐lysine adenylating enzyme and a β‐lysine binding protein involved in poly β‐lysine chain assembly in nourseothricin synthesis in Streptomyces noursei

Grammel

Pankevych

Demydchuk

et al. 2002

European Journal of Biochemistry

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Nourseothricins (syn. Streptothricins), a group of nucleoside peptides produced by several streptomycete strains, contain a poly b-lysine chain of variable length attached in amide linkage to the amino sugar moiety gulosamine of the nucleoside portion. We show that the nourseothricin-producing Streptomyces noursei contains an enzyme (NpsA) of an apparent M r 56 000 that speci®cally activates b-lysine by adenylation but does not bind to it as a thioester. Cloning and sequencing of npsA from S. noursei including its¯ank-ing DNA regions revealed that it is closely linked to the nourseothricin resistance gene nat1 and some other genes on the chromosome possibly involved in nourseothricin biosynthesis. The deduced amino-acid sequence revealed that NpsA is a stand-alone adenylation domain with similarity to the adenylation domains of nonribosomal peptide synthetases (NRPS). Further analysis revealed that S. noursei contains a b-lysine binding enzyme (NpsB) of about M r 64 100 which can be loaded by NpsA with b-lysine as a thioester. Analysis of the deduced amino-acid sequence from the gene (npsB) of NpsB showed that it consists of two domains. The N-terminal domain of 100 amino-acid residues has high similarity to PCP domains of NRPSs whereas the 450-amino-acid C-terminal domain has a high similarity to epimerization (E)-domains of NRPSs. Remarkably, in this E-domain the conserved H-H-motif is changed to H-Q, which suggests that either the domain is nonfunctional or has a specialized function. The presence of one single adenylating b-lysine activating enzyme in nourseothricin-producing streptomycete and a separate binding protein suggests an iteratively operating NRPS-module catalyses synthesis of the poly b-lysine chain.

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A β‐lysine adenylating enzyme and a β‐lysine binding protein involved in poly β‐lysine chain assembly in nourseothricin synthesis in Streptomyces noursei

Grammel

Pankevych

Demydchuk

et al. 2002

European Journal of Biochemistry

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“…AB684619 and AB684620). Nourseothricin acetyltransferase gene ( natI ), which is involved in the self-resistance, was cloned [76,77].…”

Section: Protein Synthesis Inhibitorsmentioning

confidence: 99%

Comparison of Antibiotic Resistance Mechanisms in Antibiotic-Producing and Pathogenic Bacteria

Ogawara

2019

Molecules

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Antibiotic resistance poses a tremendous threat to human health. To overcome this problem, it is essential to know the mechanism of antibiotic resistance in antibiotic-producing and pathogenic bacteria. This paper deals with this problem from four points of view. First, the antibiotic resistance genes in producers are discussed related to their biosynthesis. Most resistance genes are present within the biosynthetic gene clusters, but some genes such as paromomycin acetyltransferases are located far outside the gene cluster. Second, when the antibiotic resistance genes in pathogens are compared with those in the producers, resistance mechanisms have dependency on antibiotic classes, and, in addition, new types of resistance mechanisms such as Eis aminoglycoside acetyltransferase and self-sacrifice proteins in enediyne antibiotics emerge in pathogens. Third, the relationships of the resistance genes between producers and pathogens are reevaluated at their amino acid sequence as well as nucleotide sequence levels. Pathogenic bacteria possess other resistance mechanisms than those in antibiotic producers. In addition, resistance mechanisms are little different between early stage of antibiotic use and the present time, e.g., β-lactam resistance in Staphylococcus aureus. Lastly, guanine + cytosine (GC) barrier in gene transfer to pathogenic bacteria is considered. Now, the resistance genes constitute resistome composed of complicated mixture from divergent environments.

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“…The various members of the group differ in the length of their poly-β-lysine chains. Nourseothricin is currently being used under the name cloNAT (Werner Bioagents, Germany), and is an effective selective agent for molecular cloning technologies in fungi and plants (86)(87)(88)(89).…”

Section: Guanidine Glycoside Derivativesmentioning

confidence: 99%

Astonishing diversity of natural surfactants: 4. Fatty acid amide glycosides, their analogs and derivatives

Dembitsky

2005

Lipids

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FA amide glycosides are of great interest, especially for the medicinal and pharmaceutical industries. These biologically active natural surfactants are good prospects for future chemical preparation of compounds useful as antibiotics, anticancer agents, or for industry. More than 200 unusual and interesting natural surfactants, including their chemical structures and biological activities, are described in this review article.

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Self‐resistance of the nourseothricin‐producing strain Streptomyces noursei

Cited by 9 publications

References 16 publications

A β‐lysine adenylating enzyme and a β‐lysine binding protein involved in poly β‐lysine chain assembly in nourseothricin synthesis in Streptomyces noursei

A β‐lysine adenylating enzyme and a β‐lysine binding protein involved in poly β‐lysine chain assembly in nourseothricin synthesis in Streptomyces noursei

Comparison of Antibiotic Resistance Mechanisms in Antibiotic-Producing and Pathogenic Bacteria

Astonishing diversity of natural surfactants: 4. Fatty acid amide glycosides, their analogs and derivatives

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