Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa
The Golgi apparatus (GA) is a crucial organelle in the biosynthesis of non-cellulosic polysaccharides, glycoproteins and proteoglycans that are primarily destined for secretion to the cell surface (plasma membrane, cell wall and apoplast). Only a small proportion of the proteins involved in these pr...
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MDPI AG
2016-07-01
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Online Access: | http://www.mdpi.com/2227-7382/4/3/23 |
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author | Kristina L. Ford Tony Chin Vaibhav Srivastava Wei Zeng Monika S. Doblin Vincent Bulone Antony Bacic |
author_facet | Kristina L. Ford Tony Chin Vaibhav Srivastava Wei Zeng Monika S. Doblin Vincent Bulone Antony Bacic |
author_sort | Kristina L. Ford |
collection | DOAJ |
description | The Golgi apparatus (GA) is a crucial organelle in the biosynthesis of non-cellulosic polysaccharides, glycoproteins and proteoglycans that are primarily destined for secretion to the cell surface (plasma membrane, cell wall and apoplast). Only a small proportion of the proteins involved in these processes have been identified in plants, with the majority of their functions still unknown. The availability of a GA proteome would greatly assist plant biochemists, cell and molecular biologists in determining the precise function of the cell wall-related proteins. There has been some progress towards defining the GA proteome in the model plant system Arabidopsis thaliana, yet in commercially important species, such as either the cereals or woody species there has been relatively less progress. In this study, we applied discontinuous sucrose gradient centrifugation to partially enrich GA from suspension cell cultures (SCCs) and combined this with stable isotope labelling (iTRAQ) to determine protein sub-cellular locations. Results from a representative grass species, Italian ryegrass (Lolium multiflorum) and a dicot species, black cottonwood (Populus trichocarpa) are compared. The results confirm that membrane fractionation approaches that provide effective GA-enriched fractions for proteomic analyses in Arabidopsis are much less effective in the species examined here and highlight the complexity of the GA, both within and between species. |
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language | English |
last_indexed | 2024-04-11T11:05:36Z |
publishDate | 2016-07-01 |
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series | Proteomes |
spelling | doaj.art-b8f61c218f814de2b3b2994751de69e32022-12-22T04:28:21ZengMDPI AGProteomes2227-73822016-07-01432310.3390/proteomes4030023proteomes4030023Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpaKristina L. Ford0Tony Chin1Vaibhav Srivastava2Wei Zeng3Monika S. Doblin4Vincent Bulone5Antony Bacic6Australian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, AustraliaAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, AustraliaDivision of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, SwedenAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, AustraliaAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, AustraliaDivision of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, SwedenAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, The University of Melbourne, Victoria 3010, AustraliaThe Golgi apparatus (GA) is a crucial organelle in the biosynthesis of non-cellulosic polysaccharides, glycoproteins and proteoglycans that are primarily destined for secretion to the cell surface (plasma membrane, cell wall and apoplast). Only a small proportion of the proteins involved in these processes have been identified in plants, with the majority of their functions still unknown. The availability of a GA proteome would greatly assist plant biochemists, cell and molecular biologists in determining the precise function of the cell wall-related proteins. There has been some progress towards defining the GA proteome in the model plant system Arabidopsis thaliana, yet in commercially important species, such as either the cereals or woody species there has been relatively less progress. In this study, we applied discontinuous sucrose gradient centrifugation to partially enrich GA from suspension cell cultures (SCCs) and combined this with stable isotope labelling (iTRAQ) to determine protein sub-cellular locations. Results from a representative grass species, Italian ryegrass (Lolium multiflorum) and a dicot species, black cottonwood (Populus trichocarpa) are compared. The results confirm that membrane fractionation approaches that provide effective GA-enriched fractions for proteomic analyses in Arabidopsis are much less effective in the species examined here and highlight the complexity of the GA, both within and between species.http://www.mdpi.com/2227-7382/4/3/23Golgi apparatussub-cellular fractionationsubcellular proteomicsquantitative proteomics |
spellingShingle | Kristina L. Ford Tony Chin Vaibhav Srivastava Wei Zeng Monika S. Doblin Vincent Bulone Antony Bacic Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa Proteomes Golgi apparatus sub-cellular fractionation subcellular proteomics quantitative proteomics |
title | Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa |
title_full | Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa |
title_fullStr | Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa |
title_full_unstemmed | Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa |
title_short | Comparative “Golgi” Proteome Study of Lolium multiflorum and Populus trichocarpa |
title_sort | comparative golgi proteome study of lolium multiflorum and populus trichocarpa |
topic | Golgi apparatus sub-cellular fractionation subcellular proteomics quantitative proteomics |
url | http://www.mdpi.com/2227-7382/4/3/23 |
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