AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement
The Potexvirus Alternanthera mosaic virus (AltMV) has multifunctional triple gene block (TGB) proteins, among which our studies have focused on the properties of the TGB1 protein. The TGB1 of AltMV has functions including RNA binding, RNA silencing suppression, and cell-to-cell movement, and is know...
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| Format: | Article |
| Language: | English |
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Hanrimwon Publishing Company
2013-12-01
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| Series: | The Plant Pathology Journal |
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| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4174812/ |
| _version_ | 1819260113029955584 |
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| author | Jiryun Nam Moon Nam Hanhong Bae Cheolho Lee Bong-Chun Lee John Hammond Hyoun-Sub Lim |
| author_facet | Jiryun Nam Moon Nam Hanhong Bae Cheolho Lee Bong-Chun Lee John Hammond Hyoun-Sub Lim |
| author_sort | Jiryun Nam |
| collection | DOAJ |
| description | The Potexvirus Alternanthera mosaic virus (AltMV) has multifunctional triple gene block (TGB) proteins, among which our studies have focused on the properties of the TGB1 protein. The TGB1 of AltMV has functions including RNA binding, RNA silencing suppression, and cell-to-cell movement, and is known to form homologous interactions. The helicase domains of AltMV TGB1 were separately mutated to identify which regions are involved in homologous TGB1 interactions. The yeast two hybrid system and Bimolecular Fluorescence Complementation (BiFC) in planta were utilized to examine homologous interactions of the mutants. Helicase motif I of AltMV TGB1 was found to be critical to maintain homologous interactions. Mutations in the remaining helicase motifs did not inhibit TGB1 homologous interactions. In the absence of homologous interaction of TGB1, subcellular localization of helicase domain I mutants showed distinctively different patterns from that of WT TGB1. These results provide important information to study viral movement and replication of AltMV. |
| first_indexed | 2024-12-23T19:20:44Z |
| format | Article |
| id | doaj.art-6106e00c2b2a44048cbfcb5de211f5b6 |
| institution | Directory Open Access Journal |
| issn | 1598-2254 |
| language | English |
| last_indexed | 2024-12-23T19:20:44Z |
| publishDate | 2013-12-01 |
| publisher | Hanrimwon Publishing Company |
| record_format | Article |
| series | The Plant Pathology Journal |
| spelling | doaj.art-6106e00c2b2a44048cbfcb5de211f5b62022-12-21T17:34:11ZengHanrimwon Publishing CompanyThe Plant Pathology Journal1598-22542013-12-0129445445910.5423/PPJ.NT.04.2013.0045PPJ.NT.04.2013.0045AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell MovementJiryun Nam0Moon Nam1Hanhong Bae2Cheolho Lee3Bong-Chun Lee4John Hammond5Hyoun-Sub Lim6Department of Applied Biology, Chungnam National University, Daejeon 305-764, KoreaDepartment of Applied Biology, Chungnam National University, Daejeon 305-764, KoreaDepartment of Biological Science, Youngnam University, Gyeongsan 712-749, KoreaDepartment of Chemical and Biological Engineering, Seokyoung University, Seoul 136-704, KoreaCrop Environment Research Division, National Institute of Crop Science, RDA, Suwon 441-100, KoreaUSDA-ARS, US National Arboretum, Floral and Nursery Plants Research Unit, Beltsville, MD 20705, USADepartment of Applied Biology, Chungnam National University, Daejeon 305-764, KoreaThe Potexvirus Alternanthera mosaic virus (AltMV) has multifunctional triple gene block (TGB) proteins, among which our studies have focused on the properties of the TGB1 protein. The TGB1 of AltMV has functions including RNA binding, RNA silencing suppression, and cell-to-cell movement, and is known to form homologous interactions. The helicase domains of AltMV TGB1 were separately mutated to identify which regions are involved in homologous TGB1 interactions. The yeast two hybrid system and Bimolecular Fluorescence Complementation (BiFC) in planta were utilized to examine homologous interactions of the mutants. Helicase motif I of AltMV TGB1 was found to be critical to maintain homologous interactions. Mutations in the remaining helicase motifs did not inhibit TGB1 homologous interactions. In the absence of homologous interaction of TGB1, subcellular localization of helicase domain I mutants showed distinctively different patterns from that of WT TGB1. These results provide important information to study viral movement and replication of AltMV.http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4174812/AltMVhomologous interactionsubcellular localizationTGB1 |
| spellingShingle | Jiryun Nam Moon Nam Hanhong Bae Cheolho Lee Bong-Chun Lee John Hammond Hyoun-Sub Lim AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement The Plant Pathology Journal AltMV homologous interaction subcellular localization TGB1 |
| title | AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement |
| title_full | AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement |
| title_fullStr | AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement |
| title_full_unstemmed | AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement |
| title_short | AltMV TGB1 Nucleolar Localization Requires Homologous Interaction and Correlates with Cell Wall Localization Associated with Cell-to-Cell Movement |
| title_sort | altmv tgb1 nucleolar localization requires homologous interaction and correlates with cell wall localization associated with cell to cell movement |
| topic | AltMV homologous interaction subcellular localization TGB1 |
| url | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4174812/ |
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