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Article Addendum
EL5 is involved in root development as an anti-cell death ubiquitin ligase
Yoko Nishizawa, Shizue Katoh, Hanae Koiwai and Etsuko Katoh
volume 3 | issue 2
february 2008Pages: 148 - 150
This is an open-access article
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Ubiquitin ligase (E3) plays a central role in substrate recognition during ubiquitination, a post-translational modification of proteins. Rice EL5 is an E3 with a RING-H2 finger domain (RFD) and its transcript is upregulated by a chitin elicitor. The EL5-RFD has been intensively studied and demonstrated to exhibit E3 activity. Its three-dimensional structure was determined for the first time in plant E3, and the amino acid residues required for the interaction with the ubiquitin-conjugating enzyme (E2) were identified. Recent analyses revealed that EL5 plays a crucial role as an E3 in the maintenance of cell viability during root development in rice. In this addendum, we report that the EL5-RFD catalyzes polyubiquitination via the Lys48 residue of ubiquitin. We also discuss the possible role of EL5 as an anti-cell death enzyme. We hypothesize that EL5 might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones.
Authors
Yoko Nishizawa
Division of Plant Sciences; National Institute of Agrobiological Sciences; Tsukuba, Japan
Shizue Katoh
Division of Plant Sciences; National Institute of Agrobiological Sciences; Tsukuba, Japan
Hanae Koiwai
Division of Plant Sciences; National Institute of Agrobiological Sciences; Tsukuba, Japan
Etsuko Katoh
Division of Plant Sciences; National Institute of Agrobiological Sciences; Tsukuba, Japan
This is an open-access article
Download PDFIf the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.