Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana

<p class="IsiAbstrakIndo">Small Ubiquitin-related MOdifier (SUMO)<span lang="EN-GB"> proteins can be found in many organisms, including </span><em>A. thaliana</em><span lang="EN-GB">, which possesses 9 SUMO genes. SUMO binds to variou...

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Main Authors: Venny Santosa, Mio Nagabuchi, Sachiko Okada, Katsunori Tanaka
Format: Article
Language:English
Published: Universitas Negeri Semarang 2017-07-01
Series:Biosaintifika: Journal of Biology & Biology Education
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Online Access:https://journal.unnes.ac.id/nju/index.php/biosaintifika/article/view/9487
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author Venny Santosa
Mio Nagabuchi
Sachiko Okada
Katsunori Tanaka
author_facet Venny Santosa
Mio Nagabuchi
Sachiko Okada
Katsunori Tanaka
author_sort Venny Santosa
collection DOAJ
description <p class="IsiAbstrakIndo">Small Ubiquitin-related MOdifier (SUMO)<span lang="EN-GB"> proteins can be found in many organisms, including </span><em>A. thaliana</em><span lang="EN-GB">, which possesses 9 SUMO genes. SUMO binds to various target proteins in a reversible reaction called SUMOylation. SUMOylation participates in transcription, chromosome organization, proteins localizations and stress responses. Our study showed that RIN13 (</span>RPM1-Interacting13/At2g20310<span lang="EN-GB">) is a target of SUMOylation, which was initially found by </span>interaction<span lang="EN-GB"> between this protein and AtSCE1a (E2). Recent report showed that overexpression of RIN13 enhanced the resistance to pathogen without inducing hypersensitive response. However, the molecular interaction between RIN13 and SUMO proteins and its significance have not been studied yet. Thus, our study aimed to characterize the Interaction between RIN13 and SUMO proteins in </span><em>A. thaliana</em><span lang="EN-GB">. The result showed </span>an <span lang="EN-GB">isoform-specific SUMOylation between RIN13 and SUMO proteins. RIN13 is SUMOylated by SUMO1, 2, 3, and 5. Though expressed ubiquitously in </span><em>A.thaliana</em><span lang="EN-GB">, fluorescence microscopy showed that RIN13 localizes subcellularly in the nuclear body. Moreover, complete abolishment of SUMOylation with inactive E2 suggests the exclusion of RIN13 from nuclear body. These results showed that SUMOylation affected RIN13 localization, and indirectly influenced its interaction to other proteins and putative function. </span>This paper presents evidence of RIN13 SUMOylation. Furthermore, RIN13 function in pathogenic resistance is shown to be supported by SUMOylation. Thus, this study enhanced the understanding of SUMO in plants and served as reference to molecular studies concerning post-translational modification of SUMO.</p>
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spelling doaj-art-c7342fcc7f2743a59d6216215a87e5e62025-08-20T02:02:38ZengUniversitas Negeri SemarangBiosaintifika: Journal of Biology & Biology Education2085-191X2338-76102017-07-019216817610.15294/biosaintifika.v9i2.94876155Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thalianaVenny Santosa0Mio Nagabuchi1Sachiko Okada2Katsunori Tanaka3Universitas Kristen Satya Wacana, Graduate Program of BiologyKwansei Gakuin University, Faculty of Science and Technology, Department of BioscienceKwansei Gakuin University, Faculty of Science and Technology, Department of BioscienceKwansei Gakuin University, Faculty of Science and Technology, Department of Bioscience<p class="IsiAbstrakIndo">Small Ubiquitin-related MOdifier (SUMO)<span lang="EN-GB"> proteins can be found in many organisms, including </span><em>A. thaliana</em><span lang="EN-GB">, which possesses 9 SUMO genes. SUMO binds to various target proteins in a reversible reaction called SUMOylation. SUMOylation participates in transcription, chromosome organization, proteins localizations and stress responses. Our study showed that RIN13 (</span>RPM1-Interacting13/At2g20310<span lang="EN-GB">) is a target of SUMOylation, which was initially found by </span>interaction<span lang="EN-GB"> between this protein and AtSCE1a (E2). Recent report showed that overexpression of RIN13 enhanced the resistance to pathogen without inducing hypersensitive response. However, the molecular interaction between RIN13 and SUMO proteins and its significance have not been studied yet. Thus, our study aimed to characterize the Interaction between RIN13 and SUMO proteins in </span><em>A. thaliana</em><span lang="EN-GB">. The result showed </span>an <span lang="EN-GB">isoform-specific SUMOylation between RIN13 and SUMO proteins. RIN13 is SUMOylated by SUMO1, 2, 3, and 5. Though expressed ubiquitously in </span><em>A.thaliana</em><span lang="EN-GB">, fluorescence microscopy showed that RIN13 localizes subcellularly in the nuclear body. Moreover, complete abolishment of SUMOylation with inactive E2 suggests the exclusion of RIN13 from nuclear body. These results showed that SUMOylation affected RIN13 localization, and indirectly influenced its interaction to other proteins and putative function. </span>This paper presents evidence of RIN13 SUMOylation. Furthermore, RIN13 function in pathogenic resistance is shown to be supported by SUMOylation. Thus, this study enhanced the understanding of SUMO in plants and served as reference to molecular studies concerning post-translational modification of SUMO.</p>https://journal.unnes.ac.id/nju/index.php/biosaintifika/article/view/9487SUMORIN13SUMOylation
spellingShingle Venny Santosa
Mio Nagabuchi
Sachiko Okada
Katsunori Tanaka
Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
Biosaintifika: Journal of Biology & Biology Education
SUMO
RIN13
SUMOylation
title Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
title_full Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
title_fullStr Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
title_full_unstemmed Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
title_short Characterization of the Interaction between RIN13 (RPM1-Interacting13) and Sumo Proteins in Arabidopsis thaliana
title_sort characterization of the interaction between rin13 rpm1 interacting13 and sumo proteins in arabidopsis thaliana
topic SUMO
RIN13
SUMOylation
url https://journal.unnes.ac.id/nju/index.php/biosaintifika/article/view/9487
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AT mionagabuchi characterizationoftheinteractionbetweenrin13rpm1interacting13andsumoproteinsinarabidopsisthaliana
AT sachikookada characterizationoftheinteractionbetweenrin13rpm1interacting13andsumoproteinsinarabidopsisthaliana
AT katsunoritanaka characterizationoftheinteractionbetweenrin13rpm1interacting13andsumoproteinsinarabidopsisthaliana