pubmed-article:1347769 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0109273 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:1347769 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:1347769 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:1347769 | pubmed:dateCreated | 1992-4-23 | lld:pubmed |
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pubmed-article:1347769 | pubmed:abstractText | An intracellular symbiont harbored by the aphid bacteriocyte, a specialized fat body cell, synthesizes in vivo substantially only one protein, symbionin, which is a member of the chaperonin-60 family of molecular chaperones. Nucleotide sequence determination of the symbionin region of the endosymbiont genome revealed that it contains the two-cistron operon sym. Just like the Escherichia coli groE operon, the sym operon was dually led by a heat shock and an ordinary promoter sequence. According to the nucleotide sequence, symbionin was 85.5% identical to GroEL of E. coli at the amino acid sequence level. SymS, another protein encoded in the sym operon, which is a member of chaperonin-10, was 79.6% identical to GroES. Complementation experiments with E. coli groE mutants showed that the chaperonin-10 and chaperonin-60 genes from the endosymbiont are expressed in E. coli and that they can function as molecular chaperones together with endogenous GroEL and GroES, respectively. | lld:pubmed |
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pubmed-article:1347769 | pubmed:language | eng | lld:pubmed |
pubmed-article:1347769 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1347769 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1347769 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1347769 | pubmed:month | Mar | lld:pubmed |
pubmed-article:1347769 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:1347769 | pubmed:author | pubmed-author:NakamuraHH | lld:pubmed |
pubmed-article:1347769 | pubmed:author | pubmed-author:IshikawaHH | lld:pubmed |
pubmed-article:1347769 | pubmed:author | pubmed-author:OhtakaCC | lld:pubmed |
pubmed-article:1347769 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1347769 | pubmed:volume | 174 | lld:pubmed |
pubmed-article:1347769 | pubmed:geneSymbol | groEL | lld:pubmed |
pubmed-article:1347769 | pubmed:geneSymbol | groES | lld:pubmed |
pubmed-article:1347769 | pubmed:geneSymbol | symL | lld:pubmed |
pubmed-article:1347769 | pubmed:geneSymbol | symS | lld:pubmed |
pubmed-article:1347769 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1347769 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1347769 | pubmed:pagination | 1869-74 | lld:pubmed |
pubmed-article:1347769 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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pubmed-article:1347769 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1347769 | pubmed:articleTitle | Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants. | lld:pubmed |
pubmed-article:1347769 | pubmed:affiliation | Zoological Institute, Faculty of Science, University of Tokyo, Japan. | lld:pubmed |
pubmed-article:1347769 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1347769 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:1347769 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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