Folding and maturation of phage P22 tailspike protein in Escherichia coli strains carrying mutations in heat shock response

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dc.contributor.authorHyeyeon Koh-
dc.contributor.authorSang Chul Lee-
dc.contributor.authorMyeong Hee Yu-
dc.date.accessioned2017-04-19T08:43:57Z-
dc.date.available2017-04-19T08:43:57Z-
dc.date.issued1991-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/3101-
dc.description.abstractThe involvement of Escherichia coli molecular chaperones, GroE and DnaK proteins, in the folding and maturation of the phage P22 tailspike protein was examined. The yield of mature tailspike did not increase in the presence of excess groE gene products. Furthermore the tailspike protein folded and matured normally in an Escherichia coli host strain carrying a mutation in the groEL or dnaK gene. However, in a host strain (rpoH~) which does not have a functional heat shock transcriptional foe切r sigma32, the yield of mature tailspike was reduced substantially. The results suggest that folding and maturation of the P22 tailspike protein should require unidentified molecular chaperone(s) under the regulation of sigma32 protein.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleFolding and maturation of phage P22 tailspike protein in Escherichia coli strains carrying mutations in heat shock response-
dc.title.alternativeFolding and maturation of phage P22 tailspike protein in Escherichia coli strains carrying mutations in heat shock response-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number3-
dc.citation.endPage279-
dc.citation.startPage273-
dc.citation.volume1-
dc.contributor.affiliatedAuthorSang Chul Lee-
dc.contributor.affiliatedAuthorMyeong Hee Yu-
dc.contributor.alternativeName고혜영-
dc.contributor.alternativeName이상철-
dc.contributor.alternativeName유명희-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 1, no. 3, pp. 273-279-
dc.description.journalClassY-
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Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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