Abstract
Lysine acetylation (Kac) is a protein post-translational modification (PTM) widely found in plants that plays vital roles in metabolic pathways. Although seed germination and development are regulated by Kac, its potential function in seed ageing remains to be investigated. Our preliminary study demonstrated that Kac levels were altered during wheat seed artificial ageing. However, its specific role in this process still needs to be elucidated. Here, we performed quantitative acetylation proteomics analysis of soft wheat seeds with different germination rates during artificial ageing. A total of 175 acetylation proteins and 255 acetylation modification sites were remarkably changed. The differentially acetylated proteins were enriched in metabolism; response to harsh intracellular environment, such as ROS; protein storage and processing. Notably, expression, point mutation to mimic Kac by K to Q mutation at K80 and K138, protein purification and enzyme activity detection revealed that the Kac of ROS-scavenging glutathione transferase attenuated its activity, indicating that the defense ability of wheat seeds to stress gradually diminished, and the ageing process was inevitable. Collectively, our data provide a basis for further understanding the roles of Kac in seed ageing and might aid in the development of new techniques to prolong seed viability and food quality.
Abstract from the paper’s OpenAlex record; open copy licensed cc-by. Read at the source ↗
The text the model read, with the source record’s inline markup (italics, sub- and superscripts) rendered and its character entities decoded; quote offsets refer to the raw text.
Claims 5
Claim · model-written summary
A total of 175 acetylation proteins were remarkably changed during artificial ageing of soft wheat seeds.
Verbatim
t0“Quantitative Acetylome Analysis of Soft Wheat Seeds during Artificial Ageing”
e0“A total of 175 acetylation proteins and 255 acetylation modification sites were remarkably changed”
Claim · model-written summary
A total of 255 acetylation modification sites were remarkably changed during artificial ageing of soft wheat seeds.
Verbatim
t0“Quantitative Acetylome Analysis of Soft Wheat Seeds during Artificial Ageing”
e0“A total of 175 acetylation proteins and 255 acetylation modification sites were remarkably changed”
Claim · model-written summary
Differentially acetylated proteins were enriched in metabolism, response to ROS, and protein storage and processing.
Verbatim
t0“Quantitative Acetylome Analysis of Soft Wheat Seeds during Artificial Ageing”
e1“The differentially acetylated proteins were enriched in metabolism; response to harsh intracellular environment, such as ROS; protein storage and processing”
Claim · model-written summary
Acetylation at the K80/K138 mimic of ROS-scavenging glutathione transferase attenuated its enzyme activity.
- Taxon
- soft wheatt0
- Treatment
- K to Q mutation at K80 and K138e2
- Gene
- glutathione transferasee2
- Outcome
- enzyme activitye2
- Direction
- attenuatede2
Not reportedComparator
Verbatim
t0“Quantitative Acetylome Analysis of Soft Wheat Seeds during Artificial Ageing”
e2“Notably, expression, point mutation to mimic Kac by K to Q mutation at K80 and K138, protein purification and enzyme activity detection revealed that the Kac of ROS-scavenging glutathione transferase attenuated its activity”
Claim · model-written summary
Kac levels were altered during artificial ageing of wheat seeds in the authors preliminary study.
Verbatim
t0“Quantitative Acetylome Analysis of Soft Wheat Seeds during Artificial Ageing”
e3“Kac levels were altered during wheat seed artificial ageing”
The same questions in other papers
loss of function · soil: biology · Triticum aestivum (wheat)Results agree
2 papers in the same direction as this paper
- negative
- negative
Claims are grouped by organism, treatment and what was measured or targeted. A paper counts as positive when any of its claims in the group is positive.