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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0040648,
umls-concept:C0185117,
umls-concept:C0242772,
umls-concept:C1148673,
umls-concept:C1160534,
umls-concept:C1419388,
umls-concept:C1882531,
umls-concept:C1999216,
umls-concept:C2266866,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
2008-1-23
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pubmed:abstractText |
Recently, we have found that the accumulation of ripening inhibitor (RIN) protein increased gradually during tomato fruit ripening. Here, the recombinant protein was expressed in Escherichia coli and affinity-purified. The DNA binding activity of renatured RIN protein was tested by electrophoretic mobility shift assay. The results indicated that an optimal expression and purification system was suitable for obtaining active RIN with DNA binding activity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1347-6947
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
250-2
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pubmed:meshHeading |
pubmed-meshheading:18175904-DNA, Plant,
pubmed-meshheading:18175904-DNA-Binding Proteins,
pubmed-meshheading:18175904-Gene Expression Regulation, Plant,
pubmed-meshheading:18175904-Lycopersicon esculentum,
pubmed-meshheading:18175904-MADS Domain Proteins,
pubmed-meshheading:18175904-Open Reading Frames,
pubmed-meshheading:18175904-Plant Proteins,
pubmed-meshheading:18175904-Recombinant Proteins,
pubmed-meshheading:18175904-Repressor Proteins,
pubmed-meshheading:18175904-Transcription Factors
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pubmed:year |
2008
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pubmed:articleTitle |
Expression and DNA binding activity of the tomato transcription factor RIN (ripening inhibitor).
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pubmed:affiliation |
Laboratory of Fruit Biology, College of Food Science and Nutritional Engineering, China Agricultural University, Qinghua Donglu, Beijing, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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