Expression Analysis of the Tylosin-Biosynthetic Gene Cluster

Stratigopoulos, George; Cundliffe, Eric

doi:10.1016/s1074-5521(01)00095-3

Cited by 51 publications

(53 citation statements)

References 27 publications

(2 reference statements)

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“…In fact, the whole alp cluster seems to be a patchwork of different transfer events, with its location in the subtelomeric regions reinforcing this hypothesis (30). The homology with the tyl regulatory subcluster also suggests the existence of a similar cascade of regulation between tylosin production (38) and the orange pigment and alpomycin production. A common point is that alpV is essential for alpomycin and pigment production like its orthologue, tylS, is essential to activate tylosin production (3).…”

Section: Discussionmentioning

confidence: 69%

“…The deduced product of alpZ shares homologies with ␥-butyrolactone receptors, while AlpW exhibits similarities with transcriptional repressors such as BarB from Streptomyces virginiae (28), TylQ from S. fradiae (38), and JadR2 from Streptomyces venezuelae (47). This family of repressors corresponds to DNAbinding proteins with moderate similarity to ␥-butyrolactone receptors.…”

Section: Resultsmentioning

confidence: 99%

“…In most cases, the pathway-specific regulators play a positive role in the transcription of the biosynthetic genes, although some act as transcriptional repressors (28,38,47).…”

mentioning

confidence: 99%

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Involvement of AlpV, a New Member of the Streptomyces Antibiotic Regulatory Protein Family, in Regulation of the Duplicated Type II Polyketide Synthase alp Gene Cluster in Streptomyces ambofaciens

et al. 2005

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A type II polyketide synthase gene cluster located in the terminal inverted repeats of Streptomyces ambofaciens ATCC 23877 was shown to be responsible for the production of an orange pigment and alpomycin, a new antibiotic probably belonging to the angucycline/angucyclinone class. Remarkably, this alp cluster contains five potential regulatory genes, three of which (alpT, alpU, and alpV) encode proteins with high similarity to members of the Streptomyces antibiotic regulatory protein (SARP) family. Deletion of the two copies of alpV (one in each alp cluster located at the two termini) abolished pigment and antibiotic production, suggesting that AlpV acts as a transcriptional activator of the biosynthetic genes. Consistent with this idea, the transcription of alpA, which encodes a ketosynthase essential for orange pigment and antibiotic production, was impaired in the alpV mutant, while the expression of alpT, alpU, and alpZ, another regulatory gene encoding a ␥-butyrolactone receptor, was not significantly affected. Real-time PCR experiments showed that transcription of alpV in the wild-type strain increases dramatically after entering the transition phase. This induction precedes that of alpA, suggesting that AlpV needs to reach a threshold level to activate the expression of the structural genes. When introduced into an S. coelicolor mutant with deletions of actII-ORF4 and redD, the SARP-encoding genes regulating the biosynthesis of actinorhodin and undecylprodigiosin, respectively, alpV was able to restore actinorhodin production only. However, actII-ORF4 did not complement the alpV mutant, suggesting that AlpV and ActII-ORF4 may act in a different way.

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Section: Discussionmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

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Involvement of AlpV, a New Member of the Streptomyces Antibiotic Regulatory Protein Family, in Regulation of the Duplicated Type II Polyketide Synthase alp Gene Cluster in Streptomyces ambofaciens

et al. 2005

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“…In several cases, second tetR-type repressor genes are involved, for example, barB in Streptomyces virginiae, 28) tylQ in S. fradiae, 29) alpW in Streptomyces ambofaciens, 30) and srrB in S. rochei. 4) Differently from the low pI value characteristic of GB receptors, the second repressors have a high pI value.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Lankamycin Biosynthesis inStreptomyces rocheiby Two SARP Genes,srrYandsrrZ

Suzuki

Mochizuki

Yamamoto

et al. 2010

Bioscience, Biotechnology, and Biochemistry

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“…However, the coexpression of genes forming a functional unit is not a general observation. For example, expression studies of biosynthetic genes of the macrolide antibiotic tylosin revealed no coexpression and even no coregulation of the five genes coding for the polyketide synthases (30).…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of Chloro-β-Hydroxytyrosine, a Nonproteinogenic Amino Acid of the Peptidic Backbone of Glycopeptide Antibiotics

Puk¹,

Bischoff

Kittel³

et al. 2004

J Bacteriol

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The role of the putative P450 monooxygenase OxyD and the chlorination time point in the biosynthesis of the glycopeptide antibiotic balhimycin produced by Amycolatopsis balhimycina were analyzed. The oxyD gene is located directly downstream of the bhp (perhydrolase) and bpsD (nonribosomal peptide synthetase D) genes, which are involved in the synthesis of the balhimycin building block ␤-hydroxytyrosine (␤-HT). Reverse transcriptase experiments revealed that bhp, bpsD, and oxyD form an operon. oxyD was inactivated by an in-frame deletion, and the resulting mutant was unable to produce an active compound. Balhimycin production could be restored (i) by complementation with an oxyD gene, (ii) in cross-feeding studies using A. balhimycina JR1 (a null mutant with a block in the biosynthesis pathway of the building blocks hydroxy-and dihydroxyphenylglycine) as an excretor of the missing precursor, and (iii) by supplementation of ␤-HT in the growth medium. These data demonstrated an essential role of OxyD in the formation pathway of this amino acid. Liquid chromatography-electrospray ionization-mass spectrometry analysis indicated the biosynthesis of completely chlorinated balhimycin by the oxyD mutant when culture filtrates were supplemented with nonchlorinated ␤-HT. In contrast, supplementation with 3-chloro-␤-HT did not restore balhimycin production. These results indicated that the chlorination time point was later than the stage of free ␤-HT, most likely during heptapeptide synthesis.

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Expression Analysis of the Tylosin-Biosynthetic Gene Cluster

Cited by 51 publications

References 27 publications

Involvement of AlpV, a New Member of the Streptomyces Antibiotic Regulatory Protein Family, in Regulation of the Duplicated Type II Polyketide Synthase alp Gene Cluster in Streptomyces ambofaciens

Involvement of AlpV, a New Member of the Streptomyces Antibiotic Regulatory Protein Family, in Regulation of the Duplicated Type II Polyketide Synthase alp Gene Cluster in Streptomyces ambofaciens

Regulation of Lankamycin Biosynthesis inStreptomyces rocheiby Two SARP Genes,srrYandsrrZ

Biosynthesis of Chloro-β-Hydroxytyrosine, a Nonproteinogenic Amino Acid of the Peptidic Backbone of Glycopeptide Antibiotics

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