A Nuclear Factor That Binds to a Dyad-Symmetric Sequence with a CGTCA Motif in the 5'-Upstream Region of the Sweet Potato β-Amylase Gene

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概要

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• A nuclear extract from petioles of sweet potato protected several sites in the 5'-upstream region of a gene for β-amylase from DNase I digestion. One of these sites, located at a region around 800-base pairs upstream from the transcription start site, having an imperfect palindromic sequence of CGTCACGTCACG, was designated the R-box. The site contained tandemly duplicated CGTCA sequences, referred to below as 5'- and 3'-CGTCA. Competition experiments in gel mobility shift assays with mutant R-box oligonucleotides indicated that mutations in bases outside the 3'-CGTCA of the R-box do not severely affect the binding. By contrast, single-base substitutions in any one base of the 3'-CGTCA greatly abolished the binding even when the mutated R-boxes contained intact 5'-CGTCA. However, oligonucleotides with mutations in the 3'-CGTCA had the ability to bind the nuclear factor when additional mutations were introduced to create a partially palindromic sequence containing the CGTCA sequence in its 3'-half on the op-posite strand. These results indicate that the CGTCA sequence alone is not sufficient for the binding of the R-box binding factor (RBF) and that the RBF binds to the sequence with partial dyad symmetry that contains the CGTCA motif in its 3'-half. The optimum sequence for the binding of the RBF is suggested to be a palindromic octameric sequence TGACGTCA, which is identical to the consensus sequence of the cAMP-responsive element (CRE) of animal genes. Bacterially produced HBP-1b of wheat bound to the R-box, and its binding to mutated R-boxes was similar to that of RBF, suggesting that the RBF belongs to a family of bZIP-type plant nuclear factors that bind to CGTCA-related sequences. However, several differences between the RBF and HBP-1b were also noted.

• 日本植物生理学会の論文

著者

• NAKAMURA Kenzo

  Laboratory of Biochemistry, Graduate School of Bioagricultural Sciences, Nagoya University

• Ishiguro Sumie

  Dep. Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya Univ.

• Ishiguro S

  Nagoya Univ. Nagoya Jpn

• Ishiguro Sumie

  Dept. Botany Grad. Sch. Science Kyoto Univ.

• Ishiguro Sumie

  Department Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya

• Iwabuchi Masaki

  Department Of Botany Faculty Of Science Kyoto University Kyoto

• ISHIGURO Sumie

  Laboratory of Biochemistry, School of Agriculture, Nagoya University

• TANAKA Mihoko

  Laboratory of Biochemistry, School of Agriculture, Nagoya University

• KOJIMOTO Akihiro

  Laboratory of Biochemistry, School of Agriculture, Nagoya University

• KATO Mariko

  Laboratory of Biochemistry, School of Agriculture, Nagoya University

• Ishiguro Sumie

  Laboratory Of Biochemistry School Of Agriculture Nagoya University

• Iwabuchi Masaki

  Department Of Biology Faculty Of Science Hokkaido University

• Kojimoto Akihiro

  Laboratory Of Biochemistry School Of Agriculture Nagoya University

• Tanaka M

  Laboratory Of Biochemistry School Of Agriculture Nagoya University

• Nakamura Kenzo

  Laboratory Of Biochemistry Faculty Of Agriculture Nagoya University

• Kato Mariko

  Laboratory Of Biochemistry School Of Agriculture Nagoya University

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