Abstract
PKA (protein lysine acetylation) is a critical post-translational modification that regulates various developmental processes, including seed development. However, the acetylation events and dynamics on a proteomic scale in this process remain largely unknown, especially in rice early seed development. We report the first quantitative acetylproteomic study focused on rice early seed development by employing a mass spectral-based (MS-based), label-free approach. A total of 1817 acetylsites on 1688 acetylpeptides from 972 acetylproteins were identified in pistils and seeds at three and seven days after pollination, including 268 acetyproteins differentially acetylated among the three stages. Motif-X analysis revealed that six significantly enriched motifs, such as (DxkK), (kH) and (kY) around the acetylsites of the identified rice seed acetylproteins. Differentially acetylated proteins among the three stages, including adenosine diphosphate (ADP) -glucose pyrophosphorylases (AGPs), PDIL1-1 (protein disulfide isomerase like 1-1), hexokinases, pyruvate dehydrogenase complex (PDC) and numerous other regulators that are extensively involved in the starch and sucrose metabolism, glycolysis/gluconeogenesis, tricarboxylic acid (TCA) cycle and photosynthesis pathways during early seed development. This study greatly expanded the rice acetylome dataset, and shed novel insight into the regulatory roles of PKA in rice early seed development.
Highlights
Post-translational modification (PTM), which is a key step for functional protein maturation, refers to the covalent and generally enzymatic modification of proteins during or after protein biosynthesis
Totally 1817 acetylsites were obtained on 1688 acetylpeptides from 972 acetylproteins
The first quantitative acetylproteomic analysis focus on rice early seed development was performed by employing a mass spectral (MS)-based, label-free approach
Summary
Post-translational modification (PTM), which is a key step for functional protein maturation, refers to the covalent and generally enzymatic modification of proteins during or after protein biosynthesis. As one of the most frequent modifications, PKA (protein lysine acetylation) has been known for its critical regulatory role in various biological processes [3]. PKA was first discovered on histones, which could regulate the transcriptional level of the target genes by adjusting the status of the associated chromatin [4]. Emerging evidence has shown that PKA could occur on non-histone proteins, key metabolic enzymes related to glycolysis, tricarboxylic acid (TCA) cycle in different organisms, and photosynthesis in plants. The acetylation status affects the enzymatic activities and regulates metabolic flux through these pathways [5]. Three types of proteins are required to catalyze the reversible PKA reaction. Misfunction of some PKA-related enzymes caused severe development or growth defects in human and plants [7,8,9]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
