Pleurotus sajor-caju HSP100 complements a thermotolerance defect in hsp104 mutant Saccharomyces cerevisiae.

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dc.contributor.authorLee, Jin-Ohken_US
dc.contributor.authorJeong, Mi-Jeongen_US
dc.contributor.authorKwon, Tack-Ryunen_US
dc.contributor.authorLee, Seung-Konen_US
dc.contributor.authorByun, Myung-Oken_US
dc.contributor.authorChung, Ill-Minen_US
dc.contributor.authorPark, Soo-Chulen_US
dc.date.accessioned2006-06-01en_US
dc.date.accessioned2009-06-01T14:19:14Z
dc.date.available2006-06-01en_US
dc.date.available2009-06-01T14:19:14Z
dc.date.issued2006-06-01en_US
dc.description.abstractA putative Hsp100 gene was cloned from the fungus Pleurotus sajor-caju. mRNA expression studies demonstrated that this gene (designated PsHsp100) is highly induced by high temperature,induced less strongly by exposure to ethanol, and not induced by drought or salinity. Heat shock induction is detectable at 37 degrees C and reaches a maximum level at 42 degrees C. PsHsp100 mRNA levels sharply increased within 15 min of exposure to high temperature, and reached a maximum expression level at 2 h that was maintained for several hours. These results indicate that PsHsp100 could work at an early step in thermotolerance. To examine its function, PsHsp100 was transformed into a temperature-sensitive hsp104 deletion mutant Saccharomycetes cerivisiae strain to test the hypothesis that PsHSP100 is an protein that functions in thermotolerance. Overexpression of PsHSP100 complemented the thermotolerance defect of the hsp104 mutant yeast, allowing them being survive even at 50 degree C for 4 h. These results indicate that PsHSP100 protein is functional as an HSP100 in yeast and could play and important role in thermotolerance in P. sajor-caju.en_US
dc.description.affiliationNational Institute of Agricultural Biotechnology, Rural Development Administration, Suwon 441-707, Korea.en_US
dc.identifier.citationLee JO, Jeong MJ, Kwon TR, Lee SK, Byun MO, Chung IM, Park SC. Pleurotus sajor-caju HSP100 complements a thermotolerance defect in hsp104 mutant Saccharomyces cerevisiae. Journal of Biosciences. 2006 Jun; 31(2): 223-33en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/110745
dc.language.isoengen_US
dc.source.urihttps://www.ias.ac.in/jbiosci/index.htmlen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshFungal Proteins --classificationen_US
dc.subject.meshGene Expression Regulationen_US
dc.subject.meshGenetic Complementation Testen_US
dc.subject.meshHeat-Shock Proteins --classificationen_US
dc.subject.meshHot Temperatureen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOrganisms, Genetically Modifieden_US
dc.subject.meshPhylogenyen_US
dc.subject.meshPleurotus --geneticsen_US
dc.subject.meshRNA, Messenger --metabolismen_US
dc.subject.meshSaccharomyces cerevisiae --geneticsen_US
dc.subject.meshSaccharomyces cerevisiae Proteins --geneticsen_US
dc.subject.meshSequence Alignmenten_US
dc.titlePleurotus sajor-caju HSP100 complements a thermotolerance defect in hsp104 mutant Saccharomyces cerevisiae.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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