Characterization of three Arabidopsis homologs of human RING membrane anchor E3 ubiquitin ligase

Ora Son, Seok Keun Cho, Eun Yu Kim, Woo Taek Kim

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16 Citations (Scopus)


Ubiquitination affects diverse physiological processes in eukaryotic cells. AtRMA1 was previously identified as an Arabidopsis homolog of human RING membrane-anchor E3 ubiquitin (Ub) ligase. Here, we identified two additional AtRMA homologs, AtRMA2 and AtRMA3. The predicted AtRMA proteins contain a RING motif and a trans-membrane domain in their N-terminal and extreme C-terminal regions, respectively. Bacterially expressed AtRMAs exhibited E3 ligase activity in vitro, which was abrogated by mutation of the conserved cysteine residue in their RING domains. In vivo targeting experiments using an Arabidopsis protoplast-transfection system showed that all three AtRMAs are localized to the ER. Although RT-PCR analysis indicated that AtRMA mRNAs were expressed constitutively in all tissues examined, their promoter activities were differentially detected in a tissue-specific fashion in AtRMA-promoter::GUS transgenic Arabidopsis plants. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. We suggest that a ubiquitnation pathway involving these AtRMA E3 Ub ligases may play a role in the growth and development of Arabidopsis.

Original languageEnglish
Pages (from-to)561-569
Number of pages9
JournalPlant Cell Reports
Issue number4
Publication statusPublished - 2009 Apr

Bibliographical note

Funding Information:
Acknowledgments This work was supported by grants to W. T. K. from the Plant Diversity Research Center (21st Century Frontier Research Program funded by the Ministry of Science and Technology of Korea) and the BioGreen 21 Program (funded by Rural Development Administration of Korea).

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Plant Science


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