Abstract

BackgroundAcetylation is a crucial post-translational modification for histones, and plays a key role in gene expression regulation. Due to limited data and lack of a clear acetylation consensus sequence, a few researches have focused on prediction of lysine acetylation sites. Several systematic prediction studies have been conducted for human and yeast, but less for Arabidopsis thaliana.ResultsConcerning the insufficient observation on acetylation site, we analyzed contributions of the peptide-alignment-based distance definition and 3D structure factors in acetylation prediction. We found that traditional structure contributes little to acetylation site prediction. Identified acetylation sites of histones in Arabidopsis thaliana are conserved and cross predictable with that of human by peptide based methods. However, the predicted specificity is overestimated, because of the existence of non-observed acetylable site. Here, by performing a complete exploration on the factors that affect the acetylability of lysines in histones, we focused on the relative position of lysine at nucleosome level, and defined a new structure feature to promote the performance in predicting the acetylability of all the histone lysines in A. thaliana.ConclusionWe found a new spacial correlated acetylation factor, and defined a ε-N spacial location based feature, which contains five core spacial ellipsoid wired areas. By incorporating the new feature, the performance of predicting the acetylability of all the histone lysines in A. Thaliana was promoted, in which the previous mispredicted acetylable lysines were corrected by comparing to the peptide-based prediction.

Highlights

  • Acetylation is a crucial post-translational modification for histones, and plays a key role in gene expression regulation [1]

  • We firstly focused on the relative position of lysine at nucleosome level, and defined a new structure feature

  • Compared with human histone acetylation, identified acetylatable lysines of H2B are significantly less in Arabidopsis by Fisher Exact Test with p value less than 0.01

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Summary

Introduction

Acetylation is a crucial post-translational modification for histones, and plays a key role in gene expression regulation [1]. Many recent acetylation prediction methods were proposed to analyze Nε-acetylation, such as PAIL [5] and PredMod [6]. PredMod focuses on the major human core histones bearing a total of 56 lysines, for the wealth of information known about their PTM patterns, well-developed purification and analytical detection methods. All of the previously prediction methods are based only on the flanking peptide sequence, even through commented the structure factors, such as solvent- accessible surface area, as additional or lesssense features. Acetylation is a crucial post-translational modification for histones, and plays a key role in gene expression regulation. Due to limited data and lack of a clear acetylation consensus sequence, a few researches have focused on prediction of lysine acetylation sites. Several systematic prediction studies have been conducted for human and yeast, but less for Arabidopsis thaliana

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