Plant Physiology Preview
Published on March 20, 2003; 10.1104/pp.014035
Received September 5, 2002
Returned for revision October 22, 2002
Accepted November 30, 2002
Ethylene Regulates Monomeric GTP-Binding Protein Gene Expression and Activity in Arabidopsis
Igor E. Moshkov , Luis A.J. Mur , Galina V. Novikova , Aileen R. Smith , and Michael A. Hall *
Timiryazev Institute of Plant Physiology Russian Academy of Sciences, Botanicheskaya 35, Moscow 127276, Russia (I.E.M., G.V.N.); and Institute of Biological Sciences, University of Wales, Aberystwyth SY23 3DA, United Kingdom (L.A.J.M., A.R.S., M.A.H.)
* Corresponding author; email: mzh{at}aber.ac.uk.
Ethylene rapidly and transiently up-regulates the activity of several monomeric GTP-binding proteins (monomeric G proteins) in leaves of Arabidopsis as determined by two-dimensional gel electrophoresis and autoradiographic analyses. The activation is suppressed by the receptor-directed inhibitor 1-methylcyclopropene. In the etr1-1 mutant, constitutive activity of all the monomeric G proteins activated by ethylene is down-regulated relative to wild type, and ethylene treatment has no effect on the levels of activity. Conversely, in the ctr1-1 mutant, several of the monomeric G proteins activated by ethylene are constitutively up-regulated. However, the activation profile of ctr1-1 does not exactly mimic that of ethylene-treated wild type. Biochemical and molecular evidence suggested that some of these monomeric G proteins are of the Rab class. Expression of the genes for a number of monomeric G proteins in response to ethylene was investigated by reverse transcriptase-PCR. Rab8 and Ara3 expression was increased within 10 min of ethylene treatment, although levels fell back significantly by 40 min. In the etr1-1 mutant, expression of Rab8 was lower than wild type and unaffected by ethylene; in ctr1-1, expression of Rab8 was much higher than wild type and comparable with that seen in ethylene treatments. Expression in ctr1-1 was also unaffected by ethylene. Thus, the data indicate a role for monomeric G proteins in ethylene signal transduction.
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