Source:http://linkedlifedata.com/resource/pubmed/id/10931313
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-10-10
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pubmed:databankReference | |
pubmed:abstractText |
Anabaena strain 90 produces three hepatotoxic heptapeptides (microcystins), two seven-residue depsipeptides called anabaenopeptilide 90A and 90B, and three six-residue peptides called anabaenopeptins. The anabaenopeptilides belong to a group of cyanobacterial depsipeptides that share the structure of a six-amino-acid ring with a side-chain. Despite their similarity to known cyclic peptide toxins, no function has been assigned to the anabaenopeptilides. Degenerate oligonucleotide primers based on the conserved amino acid sequences of other peptide synthetases were used to amplify DNA from Anabaena 90, and the resulting polymerase chain reaction (PCR) products were used to identify a peptide synthetase gene cluster. Four genes encoding putative anabaenopeptilide synthetase domains were characterized. Three genes, apdA, apdB and apdD, contain two, four and one module, respectively, encoding a total of seven modules for activation and peptide bond formation of seven L-amino acids. Modules five and six also carry methyltransferase-like domains. Before the first module, there is a region similar in amino acid sequence to formyltransferases. A fourth gene (apdC), between modules six and seven, is similar in sequence to halogenase genes. Thus, the order of domains is co-linear with the positions of amino acid residues in the finished peptide. A mutant of Anabaena 90 was made by inserting a chloramphenicol resistance gene into the apdA gene. DNA amplification by PCR confirmed the insertion. Mass spectrometry analysis showed that anabaenopeptilides are not made in the mutant strain, but other peptides, such as microcystins and anabaenopeptins, are still produced by the mutant.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
156-67
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10931313-Amino Acid Sequence,
pubmed-meshheading:10931313-Anabaena,
pubmed-meshheading:10931313-Genes, Bacterial,
pubmed-meshheading:10931313-Mass Spectrometry,
pubmed-meshheading:10931313-Molecular Sequence Data,
pubmed-meshheading:10931313-Mutagenesis, Insertional,
pubmed-meshheading:10931313-Operon,
pubmed-meshheading:10931313-Peptide Synthases,
pubmed-meshheading:10931313-Peptides, Cyclic,
pubmed-meshheading:10931313-Polymerase Chain Reaction,
pubmed-meshheading:10931313-Sequence Alignment,
pubmed-meshheading:10931313-Sequence Analysis, DNA,
pubmed-meshheading:10931313-Substrate Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90.
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pubmed:affiliation |
Department of Applied Chemistry and Microbiology and Institute of Biotechnology, PO Box 56, Biocenter Viikki, FIN-00014 Helsinki University, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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