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Molecular Characterization of Two Highly Homologous Receptor-like Kinase Genes, RLK902 and RKL1, in Arabidopsis thaliana
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- TARUTANI Yoshiaki
- Department of Applied Biological Chemistry, The University of Tokyo
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- MORIMOTO Takashi
- Department of Applied Biological Chemistry, The University of Tokyo
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- SASAKI Akiko
- Department of Applied Biological Chemistry, The University of Tokyo
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- YASUDA Michiko
- Plant Functions Laboratory, RIKEN Institute
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- NAKASHITA Hideo
- Plant Functions Laboratory, RIKEN Institute
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- YOSHIDA Shigeo
- Plant Functions Laboratory, RIKEN Institute
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- YAMAGUCHI Isomaro
- Department of Applied Biological Chemistry, The University of Tokyo
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- SUZUKI Yoshihito
- Department of Applied Biological Chemistry, The University of Tokyo
Bibliographic Information
- Other Title
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- Molecular Characterization of Two Highly Homologous Receptor-like Kinase Genes,<i>RLK902</i>and<i>RKL1</i>, in<i>Arabidopsis thaliana</i>
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Description
Receptor-like kinases (RLKs) constitute a large family of signal perception molecules. We characterized two highly homologous RLK genes, RLK902 and RKL1, in Arabidopsis. RLK902 and RKL1 showed a 75% amino acid sequence identity over their entire regions. In the RLK902 pro::GUS transgenic lines, GUS activity was strong in the root tips, lateral root primordia, stipules, and floral organ abscission zones, while the RKL1 promoter activity was dominant in the stomata cells, hydathodes and trichomes of young rosette leaves, and floral organ abscission zones. Neither the rlk902 mutant line, rkl1 mutant line nor rlk902/rkl1 double-knockout mutant line showed any significant phenotypes under normal growth conditions. These results suggest that RLK902 and RKL1 might mediate the signal transduction pathway in which at least one other complementary signaling pathway to these two RLKs might exist.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 68 (9), 1935-1941, 2004
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206473000320
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- NII Article ID
- 130000030604
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 7101288
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- PubMed
- 15388970
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- Text Lang
- en
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- Article Type
- journal article
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- Data Source
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- JaLC
- NDL Search
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed