Brachypodium distachyon as a model plant toward improved biofuel crops: Search for secreted proteins involved in biogenesis and disassembly of cell wall polymers. Issue 16 (23rd July 2013)
- Record Type:
- Journal Article
- Title:
- Brachypodium distachyon as a model plant toward improved biofuel crops: Search for secreted proteins involved in biogenesis and disassembly of cell wall polymers. Issue 16 (23rd July 2013)
- Main Title:
- Brachypodium distachyon as a model plant toward improved biofuel crops: Search for secreted proteins involved in biogenesis and disassembly of cell wall polymers
- Authors:
- Douché, Thibaut
Clemente, Hélène San
Burlat, Vincent
Roujol, David
Valot, Benoît
Zivy, Michel
Pont‐Lezica, Rafael
Jamet, Elisabeth - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Polysaccharides make up about 75% of plant cell walls and can be broken down to produce sugar substrates (saccharification) from which a whole range of products can be obtained, including bioethanol. Cell walls also contain 5–10% of proteins, which could be used to tailor them for agroindustrial uses. Here we present cell wall proteomics data of <italic>Brachypodium distachyon</italic>, a model plant for temperate grasses. Leaves and culms were analyzed during active growth and at mature stage. Altogether, 559 proteins were identified by LC‐MS/MS and bioinformatics, among which 314 have predicted signal peptides. Sixty‐three proteins were shared by two organs at two developmental stages where they could play housekeeping functions. Differences were observed between organs and stages of development, especially at the level of glycoside hydrolases and oxidoreductases. Differences were also found between the known cell wall proteomes of <italic>B. distachyon</italic>, <italic>Oryza sativa</italic>, and the <italic>Arabidopsis thaliana</italic> dicot. Three glycoside hydrolases could be immunolocalized in cell walls using polyclonal antibodies against proteotypic peptides. Organ‐specific expression consistent with proteomics results could be observed as well as cell‐specific localization. Moreover, the high number of proteins of unknown function in <italic>B. distachyon</italic> cell wall<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Polysaccharides make up about 75% of plant cell walls and can be broken down to produce sugar substrates (saccharification) from which a whole range of products can be obtained, including bioethanol. Cell walls also contain 5–10% of proteins, which could be used to tailor them for agroindustrial uses. Here we present cell wall proteomics data of <italic>Brachypodium distachyon</italic>, a model plant for temperate grasses. Leaves and culms were analyzed during active growth and at mature stage. Altogether, 559 proteins were identified by LC‐MS/MS and bioinformatics, among which 314 have predicted signal peptides. Sixty‐three proteins were shared by two organs at two developmental stages where they could play housekeeping functions. Differences were observed between organs and stages of development, especially at the level of glycoside hydrolases and oxidoreductases. Differences were also found between the known cell wall proteomes of <italic>B. distachyon</italic>, <italic>Oryza sativa</italic>, and the <italic>Arabidopsis thaliana</italic> dicot. Three glycoside hydrolases could be immunolocalized in cell walls using polyclonal antibodies against proteotypic peptides. Organ‐specific expression consistent with proteomics results could be observed as well as cell‐specific localization. Moreover, the high number of proteins of unknown function in <italic>B. distachyon</italic> cell wall proteomes opens new fields of research for monocot cell walls.</p> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 13:Issue 16(2013:Aug.)
- Journal:
- Proteomics
- Issue:
- Volume 13:Issue 16(2013:Aug.)
- Issue Display:
- Volume 13, Issue 16 (2013)
- Year:
- 2013
- Volume:
- 13
- Issue:
- 16
- Issue Sort Value:
- 2013-0013-0016-0000
- Page Start:
- 2438
- Page End:
- 2454
- Publication Date:
- 2013-07-23
- Subjects:
- Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201200507 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4368.xml