pubmed-article:2160929 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2160929 | lifeskim:mentions | umls-concept:C0033809 | lld:lifeskim |
pubmed-article:2160929 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:2160929 | lifeskim:mentions | umls-concept:C0102137 | lld:lifeskim |
pubmed-article:2160929 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:2160929 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:2160929 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:2160929 | pubmed:dateCreated | 1990-7-3 | lld:pubmed |
pubmed-article:2160929 | pubmed:abstractText | The biochemical mechanism by which alpha-L-guluronate (G) residues are incorporated into alginate by Pseudomonas aeruginosa is not understood. P. aeruginosa first synthesizes GDP-mannuronate, which is used to incorporate beta-D-mannuronate residues into the polymer. It is likely that the conversion of some beta-D-mannuronate residues to G occurs by the action of a C-5 epimerase at either the monomer (e.g., sugar-nucleotide) or the polymer level. This study describes the results of a molecular genetic approach to identify a gene involved in the formation or incorporation of G residues into alginate by P. aeruginosa. Mucoid P. aeruginosa FRD1 was chemically mutagenized, and mutants FRD462 and FRD465, which were incapable of incorporating G residues into alginate, were independently isolated. Assays using a G-specific alginate lyase from Klebsiella aerogenes and 1H-nuclear magnetic resonance analyses showed that G residues were absent in the alginates secreted by these mutants. 1H-nuclear magnetic resonance analyses also showed that alginate from wild-type P. aeruginosa contained no detectable blocks of G. The mutations responsible for defective incorporation of G residues into alginate in the mutants FRD462 and FRD465 were designated algG4 and algG7, respectively. Genetic mapping experiments revealed that algG was closely linked (greater than 90%) to argF, which lies at 34 min on the P. aeruginosa chromosome and is adjacent to a cluster of genes required for alginate biosynthesis. The clone pALG2, which contained 35 kilobases of P. aeruginosa DNA that included the algG and argF wild-type alleles, was identified from a P. aeruginosa gene bank by a screening method that involved gene replacement. A DNA fragment carrying algG was shown to complement algG4 and algG7 in trans. The algG gene was physically mapped on the alginate gene cluster by subcloning and Tn501 mutagenesis. | lld:pubmed |
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pubmed-article:2160929 | pubmed:language | eng | lld:pubmed |
pubmed-article:2160929 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2160929 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2160929 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2160929 | pubmed:month | Jun | lld:pubmed |
pubmed-article:2160929 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:2160929 | pubmed:author | pubmed-author:OhmanD EDE | lld:pubmed |
pubmed-article:2160929 | pubmed:author | pubmed-author:ChitnisC ECE | lld:pubmed |
pubmed-article:2160929 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2160929 | pubmed:volume | 172 | lld:pubmed |
pubmed-article:2160929 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2160929 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2160929 | pubmed:pagination | 2894-900 | lld:pubmed |
pubmed-article:2160929 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2160929 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2160929 | pubmed:articleTitle | Cloning of Pseudomonas aeruginosa algG, which controls alginate structure. | lld:pubmed |
pubmed-article:2160929 | pubmed:affiliation | Department of Biophysics, University of California, Berkeley 94720. | lld:pubmed |
pubmed-article:2160929 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2160929 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2160929 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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