Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with calmodulin |
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Authors: | Moon Byeong Cheol Choi Man Soo Kang Yun Hwan Kim Min Chul Cheong Mi Sun Park Chan Young Yoo Jae Hyuk Koo Sung Cheol Lee Sang Min Lim Chae Oh Cho Moo Je Chung Woo Sik |
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Affiliation: | Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, Korea. |
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Abstract: | Calmodulin (CaM), a key Ca(2+) sensor in eukaryotes, regulates diverse cellular processes by interacting with many proteins. To identify Ca(2+)/CaM-mediated signaling components, we screened an Arabidopsis expression library with horseradish peroxidase-conjugated Arabidopsis calmodulin2 (AtCaM2) and isolated a homolog of the UBP6 deubiquitinating enzyme family (AtUBP6) containing a Ca(2+)-dependent CaM-binding domain (CaMBD). The CaM-binding activity of the AtUBP6 CaMBD was confirmed by CaM mobility shift assay, phosphodiesterase competition assay and site-directed mutagenesis. Furthermore, expression of AtUBP6 restored canavanine resistance to the Deltaubp6 yeast mutant. This is the first demonstration that Ca(2+) signaling via CaM is involved in ubiquitin-mediated protein degradation and/or stabilization in plants. |
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Keywords: | CaM, calmodulin AtCaM2, Arabidopsis calmodulin2 CaMBD, CaM-binding domain CaMBP, CaM-binding protein GST, glutathione S-transferase HRP, horseradish peroxidase PDE, phosphodiesterase Ub, ubiquitin UBP, ubiquitin-specific protease DUB, deubiquitination enzyme |
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