Complete nucleotide sequence of the tycA gene coding the tyrocidine synthetase 1 from<i>Bacillus brevis</i>

Weckermann, R; Fürbaß, Rainer; Marahiel, Mohamed A.

doi:10.1093/nar/16.24.11841

Cited by 104 publications

(57 citation statements)

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“…4). Analysis of the sequence revealed a long open reading frame that encodes a product with significant homology to tyrocidine synthetase 1 (33). In addition, the partial sequence upstream of the csh-293::Tn9171ac insertion revealed a potential open reading frame with similarity to gramicidin synthetase 1 (15a).…”

Section: Resultsmentioning

confidence: 99%

srfA is an operon required for surfactin production, competence development, and efficient sporulation in Bacillus subtilis

et al. 1991

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The srfA locus of BaciUlus subtilis is defined by a transposon Tn917 insertion and is required for productpon of the peptide secondary metabolite surfactin. The srfA locus was isolated by cloning the DNA flanking srfA::Tn917 insertions followed by chromosome walking. The cloned region is an operon of oyer 25 kb which covers the transcription initiation region but not the intact 3' end of srfA. csh-293, which was previously identified as a Tn9171ac mutation that impairs competence development and causes a condifoWl defect in sporulation, was known to be located in the vicinity of the srfA locus within the B. subtlis genome. The csh-293::Tn9171ac mutation was discovered to cause a defect in surfactin production and was shown to be located in the srfA operon by its cotransformation with srfA mutations and' by Southern hybridization analysis. Insertion mutations in srfA, created by the chromosomal integration of plasmids bearing overlapping srfA DNA fragments, were ex for their effects on surfactin production, competence, and sporulation. AB three processes were found to require the intact 5' half of the srfA operon, whereas the 3' half of srfA was found to be required for sporulation and surfactin production but not competence. These experiments show that srfA gene products function in B. subtilis cell specialization and differentiation.

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Section: Resultsmentioning

confidence: 99%

srfA is an operon required for surfactin production, competence development, and efficient sporulation in Bacillus subtilis

et al. 1991

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“…To determine whether this N-terminal extension has any effects on the activity of the C-terminal amino acid adenylate-forming module, we expressed the protein Srf-2 also with a short N-terminal fusion of 12 amino acids, including a (His) 6 tag. The expressed protein was designated His-Srf-2.…”

Section: Expression Of Terminal Deleted Modules From Tyrocidine Synthmentioning

confidence: 99%

“…The enzymes belong to a superfamily of adenylate-forming enzymes (6 -8). Small peptides like tyrocidine A and surfactin are formed by a nonribosomal pathway according to the thio-template mechanism (6,9). Prior to incorporation, amino acids and related compounds are activated as adenylates by cleavage of ATP and release of pyrophosphate.…”

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confidence: 99%

Substrate Specificity of Hybrid Modules from Peptide Synthetases

Elsner

Engert

Hamoen

et al. 1997

Journal of Biological Chemistry

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Homologous modules from two different peptide synthetases were analyzed for functionally equivalent regions. Hybrids between the coding regions of the phenylalanine-activating module of tyrocidine synthetase and the valine-activating module of surfactin synthetase were constructed by combining the two reading frames at various highly conserved consensus sequences. The resulting DNA fragments were expressed in Escherichia coli as C-terminal fusions to the gene encoding for the maltose-binding protein. The fusion proteins were purified, and the amino acid specificities, the acceptance of different nucleotide analogues, and the substrate binding affinities were analyzed. We found evidence for a large N-terminal domain and a short C-terminal domain of about 19 kDa within the two modules, which are separated by the sequence motif GELCIGG. The two domains could be reciprocally transferred between the two modules, and the constructed hybrid proteins showed amino acid adenylating activity. Hybrid proteins fused at various consensus motifs within the two domains were inactive, indicating that the domains may fold independently and represent complex functional units. The N-terminal domain was found to be responsible for the amino acid specificity of the modules, and it is also involved in the recognition of the ribosyl and the phosphate moieties of the nucleotide substrate. For tyrocidine synthetase I, we could confine the sites for amino acid specificity to a region of 330 residues. The C-terminal domain is essential for the enzymatic activity and has a strong impact on the specific activity of the modules.Tyrocidine synthetase and surfactin synthetase are multifunctional peptide synthetases produced by Bacillus brevis and Bacillus subtilis, respectively (1-5). The enzymes belong to a superfamily of adenylate-forming enzymes (6 -8). Small peptides like tyrocidine A and surfactin are formed by a nonribosomal pathway according to the thio-template mechanism (6, 9). Prior to incorporation, amino acids and related compounds are activated as adenylates by cleavage of ATP and release of pyrophosphate. Peptide synthetases exhibit a modular structure with several linked modules of about 100 kDa (1, 10 -16). Each module is responsible for recognition, activation, and incorporation of a specific amino acid constituent into the peptide product. Various modules of peptide synthetases have been sequenced, and several highly conserved motifs were found (7,8,11,14,(17)(18)(19). Mutagenesis and cross-linking experiments gave evidence for the involvement of most of these motifs in the binding of ATP and the adenylate forming activity (20 -23). A serine residue in the highly conserved sequence motif LGG(H/D)S at the C terminus of the modules was clearly identified as the site for covalent attachment of a phosphopantetheine cofactor (24 -26). The deletion of the cofactor attachment site in the phenylalanine-activating modules of tyrocidine synthetase I and gramicidin S synthetase I did not affect the amino acid adenylate forming activity (...

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“…), mammalian long-chain acyl-CoA synthetases (Suzuki et al 1990; Abe et al 1992;Fujino and Yamamoto 1992), luciferases from fireflies (De Wet et al 1987; Masuda et al 1989) and click beetle (Wood et al 1989), Bacillus brevis gramicidin S synthetase 1 (Honi et al 1989; Krazschmar et al 1989), B. brevis tyrocidine synthetase 1 (Weckermann et al 1988), Penicillium chrysogenum o-(L-cr-aminoadipyl)-L-cysteinyl-D-valine synthetase (Smith et al 1990; Diez et al 1990) and 4-coumarate: CoA ligases from parsley (Lozoya et al . 1988; Zhao et al 1990).…”

mentioning

confidence: 99%

Kinetic Properties and Structural Characterization of Highly Purified Acetyl-CoA Synthetase from Bovine Heart and Tissue Distribution of the Enzyme in Rat Tissues.

Ishikawa¹,

Fujino

Sakashita³

et al. 1995

Tohoku J. Exp. Med.

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Complete nucleotide sequence of the tycA gene coding the tyrocidine synthetase 1 fromBacillus brevis

Cited by 104 publications

References 2 publications

srfA is an operon required for surfactin production, competence development, and efficient sporulation in Bacillus subtilis

srfA is an operon required for surfactin production, competence development, and efficient sporulation in Bacillus subtilis

Substrate Specificity of Hybrid Modules from Peptide Synthetases

Kinetic Properties and Structural Characterization of Highly Purified Acetyl-CoA Synthetase from Bovine Heart and Tissue Distribution of the Enzyme in Rat Tissues.

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