No.42 - è¾²æ¥çç©è³æºç 究æ
No.42 - è¾²æ¥çç©è³æºç 究æ
No.42 - è¾²æ¥çç©è³æºç 究æ
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ETHYLENE-SIGNALING PATHWAY<br />
43<br />
signaling pathway turns on. However, as discussed below, the biochemical property of active<br />
ethylene receptor has not been elucidated yet.<br />
As ethylene is a tiny olefin molecule, it has been proposed that transition metals such as<br />
copper or zinc ion are required for ethylene recognition. Bleecker’s group has demonstrated that<br />
copper (I) ion is required for ethylene binding, and that Cys65 and His69 residues in the second<br />
membrane spanning domain are required for copper coordination and ethylene binding activities<br />
using recombinant ETR1 proteins expressed in the budding yeast cell (RODRIGUEZ et al. 1999).<br />
Based on these results, they proposed a model for ethylene recognition in which two Cys65<br />
residues and two His69 residues of ETR1 dimer coordinate with one copper (I) ion that is able to<br />
bind one ethylene molecule (Figure 2). These results, however, did not offer any idea on the<br />
linkage between copper requirement and ethylene receptor activity. It could be speculated at this<br />
time that ethylene receptor is active without copper ion since the conversion Cys65 to Tyr (etr1-1<br />
mutation) confers an ethylene insensitive phenotype.<br />
It is the analysis of the ran1 mutants that offered in planta functional evidence for the copper<br />
requirement for both ethylene perception and the proper conformation of ethylene receptors<br />
(HIRAYAMA et al. 1999). The ran1 mutants were isolated in a screen for mutants with altered<br />
ethylene-recognition specificities aiming to gain insight into the mechanism of ethylene<br />
Figure 2 A proposed model for ethylene recognition. Two ethylene receptor<br />
molecules constitute a functional ethylene receptor complex. Cys65<br />
and His69 on the second membrane-spanning domain coordinate<br />
with one copper (I) ion that binds one ethylene molecule.