| pubmed-article:16255248 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16255248 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:16255248 | lifeskim:mentions | umls-concept:C0600148 | lld:lifeskim |
| pubmed-article:16255248 | lifeskim:mentions | umls-concept:C1002020 | lld:lifeskim |
| pubmed-article:16255248 | lifeskim:mentions | umls-concept:C0389637 | lld:lifeskim |
| pubmed-article:16255248 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:16255248 | pubmed:dateCreated | 2005-10-31 | lld:pubmed |
| pubmed-article:16255248 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:abstractText | The insertion site of a transposon mutant of Clavibacter michiganensis subsp. michiganensis NCPPB382 was cloned and found to be located in the gene tomA encoding a member of the glycosyl hydrolase family 10. The intact gene was obtained from a cosmid library of C. michiganensis subsp. michiganensis. The deduced protein TomA (543 amino acids, 58 kDa) contains a predicted signal peptide and two domains, the N-terminal catalytic domain and a C-terminal fibronectin III-like domain. The closest well-characterized relatives of TomA were tomatinases from fungi involved in the detoxification of the tomato saponin alpha-tomatine which acts as a growth inhibitor. Growth inhibition of C. michiganensis subsp. michiganensis by alpha-tomatine was stronger in the tomA mutants than in the wild type. Tomatinase activity assayed by deglycosylation of alpha-tomatine to tomatidine was demonstrated in concentrated culture supernatants of C. michiganensis subsp. michiganensis. No activity was found with the tomA mutants. However, neither the transposon mutant nor a second mutant constructed by gene disruption was affected in virulence on the tomato cv. Moneymaker. | lld:pubmed |
| pubmed-article:16255248 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16255248 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16255248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16255248 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16255248 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16255248 | pubmed:issn | 0894-0282 | lld:pubmed |
| pubmed-article:16255248 | pubmed:author | pubmed-author:ZellermannEva... | lld:pubmed |
| pubmed-article:16255248 | pubmed:author | pubmed-author:GartemannKarl... | lld:pubmed |
| pubmed-article:16255248 | pubmed:author | pubmed-author:EichenlaubRud... | lld:pubmed |
| pubmed-article:16255248 | pubmed:author | pubmed-author:GräfenInesI | lld:pubmed |
| pubmed-article:16255248 | pubmed:author | pubmed-author:KaupOlafO | lld:pubmed |
| pubmed-article:16255248 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16255248 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:16255248 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16255248 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16255248 | pubmed:pagination | 1090-8 | lld:pubmed |
| pubmed-article:16255248 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:meshHeading | pubmed-meshheading:16255248... | lld:pubmed |
| pubmed-article:16255248 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16255248 | pubmed:articleTitle | Identification of a tomatinase in the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382. | lld:pubmed |
| pubmed-article:16255248 | pubmed:affiliation | Department of Genetechnology/Microbiology, University of Bielefeld, Universitaetsstr, Bielefeld, Germany. | lld:pubmed |
| pubmed-article:16255248 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16255248 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16255248 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16255248 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16255248 | lld:pubmed |
