Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus
| ISSN: |
1432-2242
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| Keywords: |
Movement protein ; Phosphodiesterase ; Transgenic plants
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Biology
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| Notes: |
Summary Hydrolytic activities of leaf extracts from normal and transgenic plants, with (+ MP) and without (-MP) the movement protein of tobacco mosaic virus, were examined. In the + MP transgenic plants, as compared with non-transgenic and — MP plants, higher hydrolytic activities were found on the following substrates: bis-(nitrophenyl)-phosphate (BPNPP, phosphodiesterase), p-nitrophenyl-(phenyl)-phosphate (PNPPP, nucleotidephosphodiesterase) and thymidine-3′-monophosphate p-nitrophenyl ester (T3MPP; 3′nucleotide phosphodiesterase.) The + MP plant lines, as compared with other transgenic plants, exhibited higher nucleotide-phosphodiesterase activity in the soluble as well as in the membrane fraction. Substrate concentration kinetic studies revealed the presence of a nucleotide-phospho-diesterase with a high substrate affinity in the +MP extracts in addition to the enzyme with a relatively low substrate affinity present also in the — MP transgenic plants. This “high affinity” enzyme could be removed from the soluble fraction by precipitation with anti-MP serum, indicating its possible association with the movement protein.
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| Type of Medium: |
Electronic Resource
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| URL: |