Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1)
Agbiotechnology uses genetic engineering to improve the output and value of crops. Altering the expression of the plant Type I Proton-pumping Pyrophosphatase (H+-PPase) has already proven to be a useful tool to enhance crop productivity. Despite the effective use of this gene in translational resear...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2017-09-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/article/10.3389/fpls.2017.01572/full |
| _version_ | 1819072879220752384 |
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| author | Gaston A. Pizzio Kendal D. Hirschi Roberto A. Gaxiola |
| author_facet | Gaston A. Pizzio Kendal D. Hirschi Roberto A. Gaxiola |
| author_sort | Gaston A. Pizzio |
| collection | DOAJ |
| description | Agbiotechnology uses genetic engineering to improve the output and value of crops. Altering the expression of the plant Type I Proton-pumping Pyrophosphatase (H+-PPase) has already proven to be a useful tool to enhance crop productivity. Despite the effective use of this gene in translational research, information regarding the intracellular localization and functional plasticity of the pump remain largely enigmatic. Using computer modeling several putative phosphorylation, ubiquitination and sumoylation target sites were identified that may regulate Arabidopsis H+-PPase (AVP1- Arabidopsis Vacuolar Proton-pump 1) subcellular trafficking and activity. These putative regulatory sites will direct future research that specifically addresses the partitioning and transport characteristics of this pump. We posit that fine-tuning H+-PPases activity and cellular distribution will facilitate rationale strategies for further genetic improvements in crop productivity. |
| first_indexed | 2024-12-21T17:44:44Z |
| format | Article |
| id | doaj.art-81b94c10d9684055a7ffaea3ff7d2350 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-21T17:44:44Z |
| publishDate | 2017-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-81b94c10d9684055a7ffaea3ff7d23502022-12-21T18:55:32ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2017-09-01810.3389/fpls.2017.01572278586Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1)Gaston A. Pizzio0Kendal D. Hirschi1Roberto A. Gaxiola2Center for Research in Agricultural Genomics, Consejo Superior de Investigaciones CientíficasBarcelona, SpainUSDA ARS Children’s Nutrition Research Center, Baylor College of Medicine, HoustonTX, United StatesSchool of Life Sciences, Arizona State University, TempeAZ, United StatesAgbiotechnology uses genetic engineering to improve the output and value of crops. Altering the expression of the plant Type I Proton-pumping Pyrophosphatase (H+-PPase) has already proven to be a useful tool to enhance crop productivity. Despite the effective use of this gene in translational research, information regarding the intracellular localization and functional plasticity of the pump remain largely enigmatic. Using computer modeling several putative phosphorylation, ubiquitination and sumoylation target sites were identified that may regulate Arabidopsis H+-PPase (AVP1- Arabidopsis Vacuolar Proton-pump 1) subcellular trafficking and activity. These putative regulatory sites will direct future research that specifically addresses the partitioning and transport characteristics of this pump. We posit that fine-tuning H+-PPases activity and cellular distribution will facilitate rationale strategies for further genetic improvements in crop productivity.http://journal.frontiersin.org/article/10.3389/fpls.2017.01572/fullH+-PPaseAVP1phosphorylationsumoylationubiquitinationstructural modeling |
| spellingShingle | Gaston A. Pizzio Kendal D. Hirschi Roberto A. Gaxiola Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) Frontiers in Plant Science H+-PPase AVP1 phosphorylation sumoylation ubiquitination structural modeling |
| title | Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) |
| title_full | Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) |
| title_fullStr | Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) |
| title_full_unstemmed | Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) |
| title_short | Conjecture Regarding Posttranslational Modifications to the Arabidopsis Type I Proton-Pumping Pyrophosphatase (AVP1) |
| title_sort | conjecture regarding posttranslational modifications to the arabidopsis type i proton pumping pyrophosphatase avp1 |
| topic | H+-PPase AVP1 phosphorylation sumoylation ubiquitination structural modeling |
| url | http://journal.frontiersin.org/article/10.3389/fpls.2017.01572/full |
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