Source:http://linkedlifedata.com/resource/pubmed/id/14749483
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-1-29
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pubmed:abstractText |
In Arabidopsis thaliana, a Histidine-to-Aspartate (His-->Asp) phosphorelay is involved in the signal transduction for propagation of certain stimuli, such as plant hormones. Through the phosphorelay, the type-B phospho-accepting response regulator (ARR) family members serve as DNA-binding transcriptional regulators, whose activities are most likely regulated by phosphorylation/dephosphorylation. Based on the fact that this higher plant has 11 type-B ARR family genes, we clarified the expression profiles for all of their transcripts in plants. We constructed and characterized a series of transgenic lines, each carrying a given ARR-promoter::GUS transgene. Transcripts of some type-B ARR family genes were detected more or less ubiquitously in many organs tested, while others were expressed predominantly in reproductive organs. These ARR family members were phylogenetically classified into three sub-families, the largest of which includes the well-characterized ARR1, ARR2, and ARR11. Comparative studies were conducted focusing on ARR20 and ARR21, each of which is a representative member of an uncharacterized minor sub-family. A set of transgenic lines was constructed, in each of which a C-terminal DNA-binding domain lacking the N-terminal phospho-accepting receiver of a given ARR was aberrantly overexpressed. These resulting transgenic lines, including ARR14-C-ox, ARR20-C-ox, and ARR21-C-ox, showed characteristic anomalies during development. These results are discussed with special reference to the His-->Asp phosphorelay signal transduction in A. thaliana.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/protein-histidine kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0032-0781
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
28-39
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14749483-Arabidopsis,
pubmed-meshheading:14749483-Arabidopsis Proteins,
pubmed-meshheading:14749483-Aspartic Acid,
pubmed-meshheading:14749483-DNA-Binding Proteins,
pubmed-meshheading:14749483-Gene Expression Regulation, Plant,
pubmed-meshheading:14749483-Histidine,
pubmed-meshheading:14749483-Phosphorylation,
pubmed-meshheading:14749483-Plants, Genetically Modified,
pubmed-meshheading:14749483-Protein Kinases,
pubmed-meshheading:14749483-Protein Structure, Tertiary,
pubmed-meshheading:14749483-Signal Transduction,
pubmed-meshheading:14749483-Transcription Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Comparative studies on the type-B response regulators revealing their distinctive properties in the His-to-Asp phosphorelay signal transduction of Arabidopsis thaliana.
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pubmed:affiliation |
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Chikusa-ku, Nagoya, 464-8601 Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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