Ontology type: schema:ScholarlyArticle
2010-03
AUTHORSYoshio Katakura, Ryosuke Sano, Takashi Hashimoto, Kazuaki Ninomiya, Suteaki Shioya
ABSTRACTFluorescent-labeled invertase, a hyperglycosylated mannoprotein from Saccharomyces cerevisiae, was found to bind to Lactococcus lactis IL1403 at acidic pH. Proteins on the cell wall of the bacterium affinity-purified using invertase as a ligand were identified to be heat shock proteins such as DnaK and GroEL and glycolytic enzymes such as pyruvate kinase and glyceraldehyde-3-phosphate dehydrogenase. DnaK bound to both the bacterium and yeast at pH 4 and aggregated them at above 0.1 mg/ml, whereas no significant difference between the circular dichroism spectra of DnaK at pH 4 and 7 was observed. These results indicate that the cytosolic proteins, including DnaK displayed on the cell wall, cause the lactic acid bacterium to adhere to the yeast. More... »
PAGES319-326
http://scigraph.springernature.com/pub.10.1007/s00253-009-2295-y
DOIhttp://dx.doi.org/10.1007/s00253-009-2295-y
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/19898842
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