Mol. Cells 2011; 32(4): 305-316
Published online September 9, 2011
https://doi.org/10.1007/s10059-011-0122-7
© The Korean Society for Molecular and Cellular Biology
Hee Jin Park1, Woe-Yeon Kim1, Hyeong Cheol Park1, Sang Yeol Lee1, Hans J. Bohnert1,2, and Dae-Jin Yun1,*
Correspondence to : *Correspondence: djyun@gnu.ac.kr
The traditional focus on the central dogma of molecular biology, from gene through RNA to protein, has now been replaced by the recognition of an additional mechanism. The new regulatory mechanism, post-translational modifications to proteins, can actively alter protein function or activity introducing additional levels of functional complexity by altering cellular and sub-cellular location, protein interactions and the outcome of biochemical reaction chains. Modifications by ubiquitin (Ub) and ubiquitin-like modifiers systems are conserved in all eukaryotic organisms. One of them, small ubiquitin-like modifier (SUMO) is present in plants. The SUMO mechanism includes several isoforms of proteins that are involved in reactions of sumoylation and de-sumoylation. Sumoylation affects several important processes in plants. Outstanding among those are responses to environmental stresses. These may be abiotic stresses, such as phosphate deficiency, heat, low temperature, and drought, or biotic stressses, as well including de-fense reactions to pathogen infection. Also, the regula-tions of flowering time, cell growth and develop-ment, and nitrogen assimilation have recently been added to this list. Identification of SUMO targets is material to characterize the function of sumoylation or desumoylation. Affinity purification and mass spectrometric identification have been done lately in plants. Further SUMO non-covalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be of interest to plant biologists who dissect the dynamic function of SUMO. This review will discuss results of recent insights into the role of sumoylation in plants.
Keywords Arabidopsis, SUMO, sumoylation
Mol. Cells 2011; 32(4): 305-316
Published online October 31, 2011 https://doi.org/10.1007/s10059-011-0122-7
Copyright © The Korean Society for Molecular and Cellular Biology.
Hee Jin Park1, Woe-Yeon Kim1, Hyeong Cheol Park1, Sang Yeol Lee1, Hans J. Bohnert1,2, and Dae-Jin Yun1,*
1Division of Applied Life Science (Brain Korea 21 Program), and Plant Molecular Biology and Biotechnology Research Center, Gyeongsang National University, Jinju 660-701, Korea, 2Departments of Plant Biology and of Crop Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Correspondence to:*Correspondence: djyun@gnu.ac.kr
The traditional focus on the central dogma of molecular biology, from gene through RNA to protein, has now been replaced by the recognition of an additional mechanism. The new regulatory mechanism, post-translational modifications to proteins, can actively alter protein function or activity introducing additional levels of functional complexity by altering cellular and sub-cellular location, protein interactions and the outcome of biochemical reaction chains. Modifications by ubiquitin (Ub) and ubiquitin-like modifiers systems are conserved in all eukaryotic organisms. One of them, small ubiquitin-like modifier (SUMO) is present in plants. The SUMO mechanism includes several isoforms of proteins that are involved in reactions of sumoylation and de-sumoylation. Sumoylation affects several important processes in plants. Outstanding among those are responses to environmental stresses. These may be abiotic stresses, such as phosphate deficiency, heat, low temperature, and drought, or biotic stressses, as well including de-fense reactions to pathogen infection. Also, the regula-tions of flowering time, cell growth and develop-ment, and nitrogen assimilation have recently been added to this list. Identification of SUMO targets is material to characterize the function of sumoylation or desumoylation. Affinity purification and mass spectrometric identification have been done lately in plants. Further SUMO non-covalent binding appears to have function in other model organisms and SUMO interacting proteins in plants will be of interest to plant biologists who dissect the dynamic function of SUMO. This review will discuss results of recent insights into the role of sumoylation in plants.
Keywords: Arabidopsis, SUMO, sumoylation
Chanhee Kim, Sun Ji Kim, Jinkil Jeong, Eunae Park, Eunkyoo Oh, Youn-Il Park, Pyung Ok Lim, and Giltsu Choi
Mol. Cells 2020; 43(7): 645-661 https://doi.org/10.14348/molcells.2020.0117Gyuree Kim, Sejeong Jang, Eun Kyung Yoon, Shin Ae Lee, Souvik Dhar, Jinkwon Kim, Myeong Min Lee, and Jun Lim
Mol. Cells 2018; 41(12): 1033-1044 https://doi.org/10.14348/molcells.2018.0363Laila Khaleda, Hee Jin Park, Dae-Jin Yun, Jong-Rok Jeon, Min Gab Kim, Joon-Yung Cha, and Woe-Yeon Kim
Mol. Cells 2017; 40(12): 966-975 https://doi.org/10.14348/molcells.2017.0229