A ketoreductase gene fromStreptomyces mycarofaciens 1748 DNA involved in biosynthesis of a spore pigment

1997 ◽  
Vol 40 (6) ◽  
pp. 636-641
Author(s):  
Huanzhang Xia ◽  
Yiguang Wang
Keyword(s):  
Spore Pigment

scholarly journals New Sporulation Loci in Streptomyces coelicolor A3(2)

1999 ◽  
Vol 181 (17) ◽  
pp. 5419-5425 ◽  
Author(s):  
N. Jamie Ryding ◽  
Maureen J. Bibb ◽  
Virginie Molle ◽  
Kim C. Findlay ◽  
Keith F. Chater ◽  
...  
Keyword(s):  
Phase Contrast ◽  
Streptomyces Coelicolor ◽  
Cosmid Library ◽  
Phase Contrast Microscopy ◽  
Wild Type ◽  
Chromosomal Dna ◽  
East Anglia ◽  
Wild Type Phenotype ◽  
Contrast Microscopy ◽  
Spore Pigment

ABSTRACT Sporulation mutants of Streptomyces coelicolor appear white because they are defective in the synthesis of the grey polyketide spore pigment, and such white (whi) mutants had been used to define eight sporulation loci, whiA,whiB, whiD, whiE, whiG,whiH, whiI, and whiJ (K. F. Chater, J. Gen. Microbiol. 72:9–28, 1972; N. J. Ryding, Ph.D. thesis, University of East Anglia, 1995). In an attempt to identify new whi loci, we mutagenized S. coelicolor M145 spores with nitrosoguanidine and identified 770 mutants with colonies ranging from white to medium grey. After excluding unstable strains, we examined the isolates by phase-contrast microscopy and chose 115 whi mutants with clear morphological phenotypes for further study. To exclude mutants representing cloned whi genes, self-transmissible SCP2*-derived plasmids carrying whiA, whiB,whiG, whiH, or whiJ (but notwhiD, whiE, or whiI) were introduced into each mutant by conjugation, and strains in which the wild-type phenotype was restored either partially or completely by any of these plasmids were excluded from further analysis. In an attempt to complement some of the remaining 31 whi mutants, an SCP2* library of wild-type S. coelicolor chromosomal DNA was introduced into 19 of the mutants by conjugation. Clones restoring the wild-type phenotype to 12 of the 19 strains were isolated and found to represent five distinct loci, designated whiK,whiL, whiM, whiN, andwhiO. Each of the five loci was located on the ordered cosmid library: whiL, whiM, whiN, and whiO occupied positions distinct from previously clonedwhi genes; whiK was located on the same cosmid overlap as whiD, but the two loci were shown by complementation to be distinct. The phenotypes resulting from mutations at each of these new loci are described.

scholarly journals Developmental Regulation of Transcription ofwhiE, a Locus Specifying the Polyketide Spore Pigment in Streptomyces coelicolor A3(2)

1998 ◽  
Vol 180 (9) ◽  
pp. 2515-2521 ◽  
Author(s):  
Gabriella H. Kelemen ◽  
Paul Brian ◽  
Klas Flärdh ◽  
Leony Chamberlin ◽  
Keith F. Chater ◽  
...  
Keyword(s):  
Biosynthetic Pathway ◽  
Developmental Regulation ◽  
Streptomyces Coelicolor ◽  
Colony Development ◽  
Regulation Of Transcription ◽  
Wild Type ◽  
Developmentally Regulated ◽  
Complex Locus ◽  
Spore Pigment

ABSTRACT whiE is a complex locus that specifies the polyketide spore pigment in Streptomyces coelicolor A3(2). Two divergently oriented promoters, whiEP1 andwhiEP2, were identified in the whiE gene cluster, and their activities were analyzed during colony development in wild-type and sporulation-deficient strains. Both promoters were developmentally regulated; whiEP1 and whiEP2transcripts were detected transiently at approximately the time when sporulation septa were observed in the aerial hyphae, and transcription from both promoters depended on each of the six known “early”whi genes required for sporulation septum formation (whiA, -B, -G, -H, -I, and -J). Mutation of the late sporulation-specific sigma factor gene, sigF, had no effect on the activity of whiEP1 but blocked transcription fromwhiEP2. However, ςF-containing holoenzyme was not sufficient to direct transcription of whiEP2 in vitro. The whiEP2 promoter controls expression of whiEORFVIII, encoding a putative flavin adenine dinucleotide-dependent hydroxylase that catalyzes a late tailoring step in the spore pigment biosynthetic pathway. Disruption of whiE ORFVIII causes a change in spore color, from grey to greenish (T.-W. Yu and D. A. Hopwood, Microbiology 141:2779–2791, 1995). Consistent with these observations, construction of a sigF null mutant ofS. coelicolor M145 caused the same change in spore color, showing that disruption of sigF in S. coelicolor changes the nature of the spore pigment rather than preventing its synthesis altogether.

scholarly journals CotA of Bacillus subtilis Is a Copper-Dependent Laccase

2001 ◽  
Vol 183 (18) ◽  
pp. 5426-5430 ◽  
Author(s):  
Marie-Françoise Hullo ◽  
Ivan Moszer ◽  
Antoine Danchin ◽  
Isabelle Martin-Verstraete
Keyword(s):  
Bacillus Subtilis ◽  
Coat Protein ◽  
Uv Light ◽  
Specific Substrate ◽  
Spore Coat ◽  
Wild Type ◽  
Multicopper Oxidases ◽  
Spore Pigment ◽  
Spore Coat Protein

ABSTRACT The spore coat protein CotA of Bacillus subtilisdisplays similarities with multicopper oxidases, including manganese oxidases and laccases. B. subtilis is able to oxidize manganese, but neither CotA nor other sporulation proteins are involved. We demonstrate that CotA is a laccase. Syringaldazine, a specific substrate of laccases, reacted with wild-type spores but not with ΔcotA spores. CotA may participate in the biosynthesis of the brown spore pigment, which appears to be a melanin-like product and to protect against UV light.

Cloning and disruption of a fragment of Streptomyces halstedii DNA involved in the biosynthesis of a spore pigment

Gene ◽  
1992 ◽  
Vol 112 (1) ◽  
pp. 59-65 ◽  
Author(s):  
Gloria Blanco ◽  
Ana Pereda ◽  
Carmen Méndez ◽  
JoséA. Salas
Keyword(s):  
Spore Pigment ◽  
Streptomyces Halstedii

scholarly journals A hydroxylase-like gene product contributes to synthesis of a polyketide spore pigment in Streptomyces halstedii.

1993 ◽  
Vol 175 (24) ◽  
pp. 8043-8048 ◽  
Author(s):  
G Blanco ◽  
A Pereda ◽  
P Brian ◽  
C Méndez ◽  
K F Chater ◽  
...  
Keyword(s):  
Gene Product ◽  
Spore Pigment ◽  
Streptomyces Halstedii

scholarly journals Improvement of Natamycin Production by Engineering of Phosphopantetheinyl Transferases in Streptomyces chattanoogensis L10

2013 ◽  
Vol 79 (11) ◽  
pp. 3346-3354 ◽  
Author(s):  
Hui Jiang ◽  
Yue-Yue Wang ◽  
Xin-Xin Ran ◽  
Wei-Ming Fan ◽  
Xin-Hang Jiang ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Type I ◽  
Type Ii ◽  
Carrier Proteins ◽  
Acyl Carrier Proteins ◽  
Content Type ◽  
C Terminus ◽  
Spore Pigment ◽  
Phosphopantetheinyl Transferases ◽  
Streptomyces Chattanoogensis

ABSTRACTPhosphopantetheinyl transferases (PPTases) are essential to the activities of type I/II polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) through converting acyl carrier proteins (ACPs) in PKSs and peptidyl carrier proteins (PCPs) in NRPSs from inactive apo-forms into active holo-forms, leading to biosynthesis of polyketides and nonribosomal peptides. The industrial natamycin (NTM) producer,Streptomyces chattanoogensisL10, contains two PPTases (SchPPT and SchACPS) and five PKSs. Biochemical characterization of these two PPTases shows that SchPPT catalyzes the phosphopantetheinylation of ACPs in both type I PKSs and type II PKSs, SchACPS catalyzes the phosphopantetheinylation of ACPs in type II PKSs and fatty acid synthases (FASs), and the specificity of SchPPT is possibly controlled by its C terminus. Inactivation of SchPPT inS. chattanoogensisL10 abolished production of NTM but not the spore pigment, while overexpression of the SchPPT gene not only increased NTM production by about 40% but also accelerated productions of both NTM and the spore pigment. Thus, we elucidated a comprehensive phosphopantetheinylation network of PKSs and improved polyketide production by engineering the cognate PPTase in bacteria.

Characterization of the polyketide spore pigment cluster whiESa in Streptomyces aureofaciens CCM3239

2004 ◽  
Vol 182 (5) ◽  
pp. 388-395 ◽  
Author(s):  
Renata Novakova ◽  
Jana Bistakova ◽  
Jan Kormanec
Keyword(s):  
Streptomyces Aureofaciens ◽  
Spore Pigment
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