Abstract
PKA (protein lysine acetylation) is a key post-translational modification involved in the regulation of various biological processes in rice. So far, rice acetylome data is very limited due to the highly-dynamic pattern of protein expression and PKA modification. In this study, we performed a comprehensive quantitative acetylome profile on four typical rice tissues, i.e., the callus, root, leaf, and panicle, by using a mass spectrometry (MS)-based, label-free approach. The identification of 1536 acetylsites on 1454 acetylpeptides from 890 acetylproteins represented one of the largest acetylome datasets on rice. A total of 1445 peptides on 887 proteins were differentially acetylated, and are extensively involved in protein translation, chloroplast development, and photosynthesis, flowering and pollen fertility, and root meristem activity, indicating the important roles of PKA in rice tissue development and functions. The current study provides an overall view of the acetylation events in rice tissues, as well as clues to reveal the function of PKA proteins in physiologically-relevant tissues.
Highlights
PKA (Protein lysine acetylation) refers to the substitution of an acetyl group for an active hydrogen atom on the lysine residues of a protein
The results obtained from this work aimed to provide an overall view of the acetylation events in rice tissues, as well as clues to reveal the function of PKA
Majority The of the acetylated proteins are blot analysis on the tissue proteins using afrom pan tissues, anti-acetylation protein acetylation levels non-histone proteins with a molecular weight overmajority
Summary
PKA (Protein lysine acetylation) refers to the substitution of an acetyl group for an active hydrogen atom on the lysine residues of a protein. Three types of proteins are required to catalyze the reversible. As acetylation “writers”, lysine acetyltransferases (KATs) catalyze the addition of acetyl groups from acetyl-coenzyme A (acetyl-CoA) to proteins, whereas the reversible deacetylation process is conducted by the “erasers” enzyme lysine deacetylases (KDACs). Proteins containing conserved bromodomain (BRD) or YEATS domain were found to play the roles of PKA “readers” (acetyllysine binders), as they can selectively interact with acetylated proteins [1]. Histone acetylation has been associated with chromatin remodeling and transcription activation, because a negatively-charged acetyl group could neutralize the positive charges of lysine residues, which weakens the interaction of the histone with negatively charged
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