Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition.
Chemical inhibition of the proteasome has been previously found to effectively impair pollen germination and tube growth in vitro. However, the mediators of these effects at the molecular level are unknown. By performing 2DE proteomic analysis, 24 differentially expressed protein spots, representing...
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Public Library of Science (PLoS)
2014
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oai:doaj.org-article:2f859d6dc1984ed99ef5936f6b5cabc32021-11-25T05:58:50ZProteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition.1932-620310.1371/journal.pone.0108811https://doaj.org/article/2f859d6dc1984ed99ef5936f6b5cabc32014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0108811https://doaj.org/toc/1932-6203Chemical inhibition of the proteasome has been previously found to effectively impair pollen germination and tube growth in vitro. However, the mediators of these effects at the molecular level are unknown. By performing 2DE proteomic analysis, 24 differentially expressed protein spots, representing 14 unique candidate proteins, were identified in the pollen of kiwifruit (Actinidia deliciosa) germinated in the presence of the MG132 proteasome inhibitor. qPCR analysis revealed that 11 of these proteins are not up-regulated at the mRNA level, but are most likely stabilized by proteasome inhibition. These differentially expressed proteins are predicted to function in various pathways including energy and lipid metabolism, cell wall synthesis, protein synthesis/degradation and stress responses. In line with this evidence, the MG132-induced changes in the proteome were accompanied by an increase in ATP and ROS content and by an alteration in fatty acid composition.Candida VanniniMarcella BracaleRita CrinelliValerio MarconiPaola CampomenosiMilena MarsoniValeria ScocciantiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e108811 (2014) |
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Medicine R Science Q |
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Medicine R Science Q Candida Vannini Marcella Bracale Rita Crinelli Valerio Marconi Paola Campomenosi Milena Marsoni Valeria Scoccianti Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| description |
Chemical inhibition of the proteasome has been previously found to effectively impair pollen germination and tube growth in vitro. However, the mediators of these effects at the molecular level are unknown. By performing 2DE proteomic analysis, 24 differentially expressed protein spots, representing 14 unique candidate proteins, were identified in the pollen of kiwifruit (Actinidia deliciosa) germinated in the presence of the MG132 proteasome inhibitor. qPCR analysis revealed that 11 of these proteins are not up-regulated at the mRNA level, but are most likely stabilized by proteasome inhibition. These differentially expressed proteins are predicted to function in various pathways including energy and lipid metabolism, cell wall synthesis, protein synthesis/degradation and stress responses. In line with this evidence, the MG132-induced changes in the proteome were accompanied by an increase in ATP and ROS content and by an alteration in fatty acid composition. |
| format |
article |
| author |
Candida Vannini Marcella Bracale Rita Crinelli Valerio Marconi Paola Campomenosi Milena Marsoni Valeria Scoccianti |
| author_facet |
Candida Vannini Marcella Bracale Rita Crinelli Valerio Marconi Paola Campomenosi Milena Marsoni Valeria Scoccianti |
| author_sort |
Candida Vannini |
| title |
Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| title_short |
Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| title_full |
Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| title_fullStr |
Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| title_full_unstemmed |
Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| title_sort |
proteomic analysis of mg132-treated germinating pollen reveals expression signatures associated with proteasome inhibition. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2014 |
| url |
https://doaj.org/article/2f859d6dc1984ed99ef5936f6b5cabc3 |
| work_keys_str_mv |
AT candidavannini proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT marcellabracale proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT ritacrinelli proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT valeriomarconi proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT paolacampomenosi proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT milenamarsoni proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition AT valeriascoccianti proteomicanalysisofmg132treatedgerminatingpollenrevealsexpressionsignaturesassociatedwithproteasomeinhibition |
| _version_ |
1718414329641959424 |