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. 1988 Dec;88(4):996–998. doi: 10.1104/pp.88.4.996

Binding of Spermidine to a Unique Protein in Thin-Layer Tobacco Tissue Culture 1

Akiva Apelbaum 1,2,3,2, Zoe N Canellakis 1,2,3, Philip B Applewhite 1,2,3, Ravindar Kaur-Sawhney 1,2,3, Arthur W Galston 1,2,3
PMCID: PMC1055703  PMID: 11537444

Abstract

The mechanism by which spermidine induces the appearance of floral buds in thin-layer tobacco (Nicotiana tabacum) tissue culture was studied by following the fate of the radioactive compound. [3H]Spermidine was taken up rapidly by the tissue, and after a brief lag, a portion was bound to trichloroacetic acid precipitable macromolecules. Such binding increased to a maximum on day 4 of culture, coinciding with the onset of bud differentiation, and declined thereafter until shortly before flowering. About 82% of the label in the trichloroacetic acid precipitate remained as spermidine, 14% was metabolized to putrescine, 3% to spermine, and 1% to γ-aminobutyric acid. Spermidine was covalently bound to a protein with a molecular size of about 18 kilodaltons. Hydrolysis of this protein and analysis of the labeled entities revealed 81% spermidine, 16% putrescine, and 3% spermine. This post-translational modification of a unique protein by attachment of spermidine may be causally connected to the appearance of flower buds in thin-layer tobacco cultures.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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