אסיף מאגר המחקר החקלאי

Phosphodiesterase activities in transgenic tobacco plants associated with the movement protein of tobacco mosaic virus

Year:

1992

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Volume :

84

Co-Authors:

Perl, M., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Gafni, R., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States
Beachy, R.N., Department of Biology, Washington University, Box 1137, St. Louis, 63130, MO, United States

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Abstract:

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. © 1992 Springer-Verlag.

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