In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana
Microtubules are essential components of cytoskeleton, rigid hollow rods approximately 25 nm in diameter. Microtubules are dynamic structures being continuously assembled and disassembled within the cell. The basic building blocks of microtubules are heterodimers of globular α- and β-tubulin subunit...
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| Format: | Article |
| Language: | English |
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International Academy of Ecology and Environmental Sciences
2014-06-01
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| Series: | Network Biology |
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| Online Access: | http://www.iaees.org/publications/journals/nb/articles/2014-4(2)/prediction-of-three-dimensional-structure-and-interactome-analysis.pdf |
| _version_ | 1818689044376190976 |
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| author | Jasmin Sutkovic Mohamed Ragab Abdel Gawwad |
| author_facet | Jasmin Sutkovic Mohamed Ragab Abdel Gawwad |
| author_sort | Jasmin Sutkovic |
| collection | DOAJ |
| description | Microtubules are essential components of cytoskeleton, rigid hollow rods approximately 25 nm in diameter. Microtubules are dynamic structures being continuously assembled and disassembled within the cell. The basic building blocks of microtubules are heterodimers of globular α- and β-tubulin subunits In Arabidopsis thaliana tubulin subunits are encoded by small gene families, six for α-tubulin and nine for β-tubulin.Both α- and β-tubulin bind GTP, which functions analogously to the ATP bound to actin to regulate polymerization. It is shown that tubulin α forms hydrogen bonds with the GTPase domain of b-tubulin. Multiple sequence alignment revealed high similarity between the family subunits. Due to the missing of three dimensional structuresin A. thaliana, structural models were predicted and validated. Additionally, protein domains search revealed that all tubulin α family subunits contain GTPase domain as the tubulin C terminal domain, confirming previous research. Finally the interactome analysis revealed several interactomes. AtTUA6 shows strong interaction with embryosac development arrest 10 protein (EDA10), involved in stimulating the exchange of guanyl nucleotides, enabling the replacement of GDP by GTP in association with a GTPases. |
| first_indexed | 2024-12-17T12:03:51Z |
| format | Article |
| id | doaj.art-f7ebf3abbce44f6d87700b57f1404700 |
| institution | Directory Open Access Journal |
| issn | 2220-8879 2220-8879 |
| language | English |
| last_indexed | 2024-12-17T12:03:51Z |
| publishDate | 2014-06-01 |
| publisher | International Academy of Ecology and Environmental Sciences |
| record_format | Article |
| series | Network Biology |
| spelling | doaj.art-f7ebf3abbce44f6d87700b57f14047002022-12-21T21:49:43ZengInternational Academy of Ecology and Environmental SciencesNetwork Biology2220-88792220-88792014-06-01424757In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thalianaJasmin Sutkovic0Mohamed Ragab Abdel Gawwad1Genetics and Bioengineering Department, International University of Sarajevo, Ilidza, 71220 Bosnia and HerzegovinaGenetics and Bioengineering Department, International University of Sarajevo, Ilidza, 71220 Bosnia and HerzegovinaMicrotubules are essential components of cytoskeleton, rigid hollow rods approximately 25 nm in diameter. Microtubules are dynamic structures being continuously assembled and disassembled within the cell. The basic building blocks of microtubules are heterodimers of globular α- and β-tubulin subunits In Arabidopsis thaliana tubulin subunits are encoded by small gene families, six for α-tubulin and nine for β-tubulin.Both α- and β-tubulin bind GTP, which functions analogously to the ATP bound to actin to regulate polymerization. It is shown that tubulin α forms hydrogen bonds with the GTPase domain of b-tubulin. Multiple sequence alignment revealed high similarity between the family subunits. Due to the missing of three dimensional structuresin A. thaliana, structural models were predicted and validated. Additionally, protein domains search revealed that all tubulin α family subunits contain GTPase domain as the tubulin C terminal domain, confirming previous research. Finally the interactome analysis revealed several interactomes. AtTUA6 shows strong interaction with embryosac development arrest 10 protein (EDA10), involved in stimulating the exchange of guanyl nucleotides, enabling the replacement of GDP by GTP in association with a GTPases.http://www.iaees.org/publications/journals/nb/articles/2014-4(2)/prediction-of-three-dimensional-structure-and-interactome-analysis.pdf3D structureinteractomemicrotubulestubulin αfunctional annotation |
| spellingShingle | Jasmin Sutkovic Mohamed Ragab Abdel Gawwad In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana Network Biology 3D structure interactome microtubules tubulin α functional annotation |
| title | In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana |
| title_full | In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana |
| title_fullStr | In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana |
| title_full_unstemmed | In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana |
| title_short | In silico prediction of three-dimensional structure and interactome analysis of Tubulin α subfamily of Arabidopsis thaliana |
| title_sort | in silico prediction of three dimensional structure and interactome analysis of tubulin α subfamily of arabidopsis thaliana |
| topic | 3D structure interactome microtubules tubulin α functional annotation |
| url | http://www.iaees.org/publications/journals/nb/articles/2014-4(2)/prediction-of-three-dimensional-structure-and-interactome-analysis.pdf |
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