Biochemical and genetic studies on histidine deficient mutants of Streptomyces coelicolor.
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Biochemical and genetic studies on histidine deficient mutants of Streptomyces coelicolor.

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Published by Waltman in Delft .
Written in English

Subjects:

  • Streptomyces coelicolor.,
  • Histidine.,
  • Mutagenesis.

Book details:

Classifications
LC ClassificationsQR82.A35 K48
The Physical Object
Pagination80 p.
Number of Pages80
ID Numbers
Open LibraryOL4346005M
LC Control Number78387658

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  Biochemical and genetic data indicate that in Streptomyces coelicolor A3(2) the majority of the genes involved in the biosynthesis of histidine are clustered in a small region of the chromosome [Carere et al., Mol. Gen. Genet. () –; Russi et al., Mol. Gen. Genet. () –]. To investigate the structural organization and the regulation of these genes, we have Cited by: Histidine-requiring mutants were maximal among the mutants from the wild-type. Among nucleic-acid-deficient mutants, only one hypoxanthine-requiring strain was isolated. Vitamin-deficient mutants were not obtained from the wild-type S. indicus. These were, however, isolated by irradiating the mutant strains MT-1o and y by: 3.   The genetic organization of the genes in the vicinity of ohkAsp were found to be conserved among Streptomyces species as that in its homologs from S. coelicolor, and S. avermitilis and the only region that differed was the LCR (Lu et al., ). Being bacterial histidine kinase belonging to a transmembrane category, OhkAsp is unique for Cited by: 4. In this study, we constructed mutants of Streptomyces coelicolor A3(2), in which either the MSH or ERG biosynthetic gene was disrupted, and examined their phenotypes. A mshC (SCO)-disruptant.

coelicolor ch or streptomyces lividans tk 64 and e. coli Intergeneric conjugation remains a robust means to introduce DN A into Streptomyces species from an E. coli host. Merrick MJ () A morphological and genetic mapping study of bald colony mutants of () Ultrastructural studies on sporulation in wild-type and white colony mutants of Streptomyces coelicolor. J Gen Microbiol – Construction and phenotypes of double sporulation deficient mutants in Streptomyces coelicolor A 3(2). J Gen.   Streptomyces reticuli produces a unique kDa Avicel-binding protein, named AbpS that protrudes from its cell-wall. Biochemical studies with generated and purified mutant proteins complemented by investigations of designed Streptomyces mutant strains allowed assigning the relevant features of protein-domains. Amino acid residues. The whiD locus, which is required for the differentiation of Streptomyces coelicolor aerial hyphae into mature spore chains, was localized by map-based cloning to the overlap between cosmids 6G4 and D63 of the minimal ordered library of Redenbach et al. (M. Redenbach et al., Mol. Microbiol. –96, ). Subcloning and sequencing showed that whiD encodes a homologue of WhiB, a protein.

The Streptomycetes are industrially widely used microorganisms due to their ability to produce numerous different chemical compounds. These show very varied effects upon other living systems, and result from profound and subtle biochemical and morphological differentiation during the streptomycete life cycle. Streptomyces coelicolor mutant RF, isolated as a revertant of a histidine auxotroph after mutagenic treatment with N-methylN'-nitro-N-nitrosoguanidine, was found to accumulate L-histidine. The mutant was sensitive to 2-thiazo-lealanine and L-2,4-diaminobutyric. Merrick MJ. A morphological and genetic mapping study of bald colony mutants of Streptomyces coelicolor. J Gen Microbiol. Oct; 96 (2)– Narva KE, Feitelson JS. Nucleotide sequence and transcriptional analysis of the redD locus of Streptomyces coelicolor A3(2). J Bacteriol. Jan; (1)– [PMC free article]. The inactivation and mutagenic effets of nitrous acid on a non-acid-fast strain ofMycobacterium phlei were studied. It was found that m NaNO2 at pH may be used for the induction of auxotrophic mutants, scotochromogenic and achromogenic mutants and STM-resistant mutants. Three doubly auxotrophic mutants, three mutants requiring amino acids and three mutants depending on vitamins .