Primary structure of a hormonally regulated beta-glucanase of Nicotiana plumbaginifolia |
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Authors: | M De Loose T Alliotte G Gheysen C Genetello J Gielen P Soetaert M Van Montagu D Inzé |
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Institution: | Laboratorium voor Genetica, Rijksuniversiteit Gent, Belgium. |
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Abstract: | A cDNA clone for a hormonally regulated beta-glucanase from Nicotiana plumbaginifolia has been isolated by using an oligodeoxynucleotide probe, synthesized to match the previously determined N-terminal amino acid sequence. The cDNA has the complete sequence of the mature protein and contains at least part of a hydrophobic signal peptide. At the amino acid level, the beta-glucanase of N. plumbaginifolia is 73% homologous to a beta(1,3)-glucanase from tobacco and 52% homologous to a beta(1,3;1,4)-glucanase from barley. Southern-blot analysis clearly demonstrated that N. plumbaginifolia contains at least two related genes encoding beta-glucanase. The extent of the complete signal peptide of the cloned beta-glucanase was determined by sequencing part of the corresponding gene. Northern analysis showed that the expression of the beta-glucanase gene is influenced by auxins and cytokinins. |
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