A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids.
The plastid-localized methylerythritol phosphate (MEP) pathway synthesizes the isoprenoid precursors for the production of essential photosynthesis-related compounds and hormones. We have identified an Arabidopsis thaliana mutant, rif1, in which posttranscriptional upregulation of MEP pathway enzyme...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2008
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| _version_ | 1826298023335952384 |
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| author | Flores-Pérez, U Sauret-Güeto, S Gas, E Jarvis, P Rodríguez-Concepción, M |
| author_facet | Flores-Pérez, U Sauret-Güeto, S Gas, E Jarvis, P Rodríguez-Concepción, M |
| author_sort | Flores-Pérez, U |
| collection | OXFORD |
| description | The plastid-localized methylerythritol phosphate (MEP) pathway synthesizes the isoprenoid precursors for the production of essential photosynthesis-related compounds and hormones. We have identified an Arabidopsis thaliana mutant, rif1, in which posttranscriptional upregulation of MEP pathway enzyme levels is caused by the loss of function of At3g47450, a gene originally reported to encode a mitochondrial protein related to nitric oxide synthesis. However, we show that nitric oxide is not involved in the regulation of the MEP pathway and that the encoded protein is a plastid-targeted homolog of the Bacillus subtilis YqeH protein, a GTPase required for proper ribosome assembly. Consistently, in rif1 seedlings, decreased levels of plastome-encoded proteins were observed, with the exception of ClpP1, a catalytic subunit of the plastidial Clp protease complex. The unexpected accumulation of ClpP1 in plastids with reduced protein synthesis suggested a compensatory mechanism in response to decreased Clp activity levels. In agreement, a negative correlation was found between Clp protease activity and MEP pathway enzyme levels in different experiments, suggesting that Clp-mediated degradation of MEP pathway enzymes might be a mechanism used by individual plastids to finely adjust plastidial isoprenoid biosynthesis to their functional and physiological states. |
| first_indexed | 2024-03-07T04:40:30Z |
| format | Journal article |
| id | oxford-uuid:d176cedf-dcc6-4c00-8942-8063a9a8dcf2 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:40:30Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:d176cedf-dcc6-4c00-8942-8063a9a8dcf22022-03-27T07:57:12ZA mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d176cedf-dcc6-4c00-8942-8063a9a8dcf2EnglishSymplectic Elements at Oxford2008Flores-Pérez, USauret-Güeto, SGas, EJarvis, PRodríguez-Concepción, MThe plastid-localized methylerythritol phosphate (MEP) pathway synthesizes the isoprenoid precursors for the production of essential photosynthesis-related compounds and hormones. We have identified an Arabidopsis thaliana mutant, rif1, in which posttranscriptional upregulation of MEP pathway enzyme levels is caused by the loss of function of At3g47450, a gene originally reported to encode a mitochondrial protein related to nitric oxide synthesis. However, we show that nitric oxide is not involved in the regulation of the MEP pathway and that the encoded protein is a plastid-targeted homolog of the Bacillus subtilis YqeH protein, a GTPase required for proper ribosome assembly. Consistently, in rif1 seedlings, decreased levels of plastome-encoded proteins were observed, with the exception of ClpP1, a catalytic subunit of the plastidial Clp protease complex. The unexpected accumulation of ClpP1 in plastids with reduced protein synthesis suggested a compensatory mechanism in response to decreased Clp activity levels. In agreement, a negative correlation was found between Clp protease activity and MEP pathway enzyme levels in different experiments, suggesting that Clp-mediated degradation of MEP pathway enzymes might be a mechanism used by individual plastids to finely adjust plastidial isoprenoid biosynthesis to their functional and physiological states. |
| spellingShingle | Flores-Pérez, U Sauret-Güeto, S Gas, E Jarvis, P Rodríguez-Concepción, M A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title | A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title_full | A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title_fullStr | A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title_full_unstemmed | A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title_short | A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids. |
| title_sort | mutant impaired in the production of plastome encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in arabidopsis plastids |
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