Abstract
Exposure to elevated temperatures and relative humidity expedites the seed aging process, finally leading to seed viability loss. In this context, certain proteins play a pivotal role in safeguarding the longevity of seeds. However, the seedproteomic response to loss viability in Salvia hispanica L., commonly known as chia, remains incompletely understood. This work explores the application of proteomics as a potent tool for uncovering molecular responses to viability loss caused by artificial aging in two chia genotypes, WN and MN. By using a quantitative label-free proteomics analysis (LC-MS/MS), 1787 proteins wereidentified in chia seeds at a 95% confidence level, including storage proteins, heat shock proteins (HSPs), late embryogenesis abundant proteins (LEA),oleosins, reactive oxygen species (ROS)-related enzymes, and ribosomal proteins. A relatively low percentage of exclusive proteins were identified in viable and non-viable seeds. However, proteins exhibiting differential abundancebetween samples indicated variations in the genotype and physiological status. Specifically, the WN genotype showed 130 proteins with differential abundancecomparing viable and non-viable seeds, while MN displayed changes in the abundance of 174 proteins. While both showed a significant decrease in keyproteins responsible for maintaining seed functionality, longevity, and vigor withhigh-temperature and humidity conditions, such as LEA proteins or HSPs, ROS, and oleosins, distinct responses between genotypes were noted, particularly in ribosomal proteins that were accumulated in MN and diminished in WN seeds. Overall, the results emphasize the importance of evaluating changes in proteins of viable and non-viable seeds as they offer valuable insights into the underlying biological mechanisms responsible for the maintenance of chia seed integrity throughout high-temperature and humidity exposure.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.