HvPap-1 C1A Protease and HvCPI-2 Cystatin Contribute to Barley Grain Filling and Germination. Issue 4 (24th February 2016)
- Record Type:
- Journal Article
- Title:
- HvPap-1 C1A Protease and HvCPI-2 Cystatin Contribute to Barley Grain Filling and Germination. Issue 4 (24th February 2016)
- Main Title:
- HvPap-1 C1A Protease and HvCPI-2 Cystatin Contribute to Barley Grain Filling and Germination
- Authors:
- Diaz-Mendoza, Mercedes
Dominguez-Figueroa, Jose D.
Velasco-Arroyo, Blanca
Cambra, Ines
Gonzalez-Melendi, Pablo
Lopez-Gonzalvez, Angeles
Garcia, Antonia
Hensel, Goetz
Kumlehn, Jochen
Diaz, Isabel
Martinez, Manuel - Abstract:
- Abstract : Over-expressing or silencing proteases or their inhibitors alter the metabolite composition of the grain and modify the germination process in barley Abstract: Proteolysis is an essential process throughout the mobilization of storage proteins in barley ( Hordeum vulgare ) grains during germination. It involves numerous types of enzymes, with C1A Cys proteases the most abundant key players. Manipulation of the proteolytic machinery is a potential way to enhance grain yield and quality, and it could influence the mobilization of storage compounds along germination. Transgenic barley plants silencing or over-expressing the cathepsin F-like HvPap-1 Cys protease show differential accumulation of storage molecules such as starch, proteins, and free amino acids in the grain. It is particularly striking that the HvPap-1 artificial microRNA lines phenotype show a drastic delay in the grain germination process. Alterations to the proteolytic activities in the over-expressing and knock-down grains associated with changes in the level of expression of several C1A peptidases were also detected. Similarly, down-regulating cystatin Icy-2, one of the proteinaceous inhibitors of the cathepsin F-like protease, also has important effects on grain filling. However, the ultimate physiological influence of manipulating a peptidase or an inhibitor cannot be always predicted, since the plant tries to compensate the modified proteolytic effects by modulating the expression of some otherAbstract : Over-expressing or silencing proteases or their inhibitors alter the metabolite composition of the grain and modify the germination process in barley Abstract: Proteolysis is an essential process throughout the mobilization of storage proteins in barley ( Hordeum vulgare ) grains during germination. It involves numerous types of enzymes, with C1A Cys proteases the most abundant key players. Manipulation of the proteolytic machinery is a potential way to enhance grain yield and quality, and it could influence the mobilization of storage compounds along germination. Transgenic barley plants silencing or over-expressing the cathepsin F-like HvPap-1 Cys protease show differential accumulation of storage molecules such as starch, proteins, and free amino acids in the grain. It is particularly striking that the HvPap-1 artificial microRNA lines phenotype show a drastic delay in the grain germination process. Alterations to the proteolytic activities in the over-expressing and knock-down grains associated with changes in the level of expression of several C1A peptidases were also detected. Similarly, down-regulating cystatin Icy-2, one of the proteinaceous inhibitors of the cathepsin F-like protease, also has important effects on grain filling. However, the ultimate physiological influence of manipulating a peptidase or an inhibitor cannot be always predicted, since the plant tries to compensate the modified proteolytic effects by modulating the expression of some other peptidases or their inhibitors. … (more)
- Is Part Of:
- Plant physiology. Volume 170:Issue 4(2016)
- Journal:
- Plant physiology
- Issue:
- Volume 170:Issue 4(2016)
- Issue Display:
- Volume 170, Issue 4 (2016)
- Year:
- 2016
- Volume:
- 170
- Issue:
- 4
- Issue Sort Value:
- 2016-0170-0004-0000
- Page Start:
- 2511
- Page End:
- 2524
- Publication Date:
- 2016-02-24
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.15.01944 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
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