In Arabidopsis thaliana, 1-aminocyclopropane-1-carboxylate synthase (ACS) is encoded by a multigene family consisting of at least five members whose expression is induced by hormones, developmental signals, and protein synthesis inhibition. Li+, known to interfere with the phosphoinositide (PI) second messenger system by inhibiting the activity of inositol-phosphate phosphatases, is one of the strongest inducers of ACC synthase activity in plants. Treatment of etiolated Arabidopsis seedlings with LiCl results in a rapid induction of the ACS5 gene. Also, LiCl represses the cycloheximide (CHX)-induced accumulation of the ACS2 mRNA. The effects of Li+ on the expression of ACS5 and ACS2 are specific, dose-dependent, and can be reversed by Ca2+ and mimicked by the protein kinase inhibitor K-252a. The results suggest that the regulation of some ACS genes by various inducers may involve protein kinase activity, which in turn may be controlled through an inositol 1,4,5-triphosphate (IP3)-mediated Ca2+ mobilization. Since plants contain no Li+, the cation appears to unmask pre-existing biochemical capacity that may be utilized by various unknown transducers during plant growth and development.
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http://purl.uniprot.org/cit... | rdf:type | uniprot:Journal_Citation | lld:uniprot |
http://purl.uniprot.org/cit... | rdfs:comment | In Arabidopsis thaliana, 1-aminocyclopropane-1-carboxylate synthase (ACS) is encoded by a multigene family consisting of at least five members whose expression is induced by hormones, developmental signals, and protein synthesis inhibition. Li+, known to interfere with the phosphoinositide (PI) second messenger system by inhibiting the activity of inositol-phosphate phosphatases, is one of the strongest inducers of ACC synthase activity in plants. Treatment of etiolated Arabidopsis seedlings with LiCl results in a rapid induction of the ACS5 gene. Also, LiCl represses the cycloheximide (CHX)-induced accumulation of the ACS2 mRNA. The effects of Li+ on the expression of ACS5 and ACS2 are specific, dose-dependent, and can be reversed by Ca2+ and mimicked by the protein kinase inhibitor K-252a. The results suggest that the regulation of some ACS genes by various inducers may involve protein kinase activity, which in turn may be controlled through an inositol 1,4,5-triphosphate (IP3)-mediated Ca2+ mobilization. Since plants contain no Li+, the cation appears to unmask pre-existing biochemical capacity that may be utilized by various unknown transducers during plant growth and development. | lld:uniprot |
http://purl.uniprot.org/cit... | skos:exactMatch | http://purl.uniprot.org/pub... | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:name | Plant J. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Liang X.-W. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Shen N.F. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:author | Theologis A. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:date | 1996 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:pages | 1027-1036 | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:title | Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression in Arabidopsis thaliana. | lld:uniprot |
http://purl.uniprot.org/cit... | uniprot:volume | 10 | lld:uniprot |
http://purl.uniprot.org/cit... | dc-term:identifier | doi:10.1046/j.1365-313X.1996.10061027.x | lld:uniprot |
uniprot-protein:Q37001 | uniprot:citation | http://purl.uniprot.org/cit... | lld:uniprot |
http://linkedlifedata.com/r... | uniprot:citation | http://purl.uniprot.org/cit... | lld:uniprot |
http://linkedlifedata.com/r... | rdf:object | http://purl.uniprot.org/cit... | lld:uniprot |