Related Experiment Video
Updated: Oct 19, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
STALLION: a stacking-based ensemble learning framework for prokaryotic lysine acetylation site prediction
Shaherin Basith1, Gwang Lee2, Balachandran Manavalan1
1Department of Physiology, Ajou University School of Medicine, Republic of Korea.
This study introduces STALLION, a novel predictor for identifying protein lysine acetylation sites in prokaryotes. STALLION accurately identifies these crucial regulatory sites, outperforming existing methods.
Area of Science:
- Biochemistry and Molecular Biology
- Bioinformatics
- Computational Biology
Background:
- Protein post-translational modification (PTM) regulates cellular functions; lysine acetylation (Kace) is a key PTM.
- Identifying Kace sites is vital for understanding cellular processes and disease states.
- Existing computational methods for Kace site prediction have limitations, especially for prokaryotic species.
Purpose of the Study:
- To develop a novel, accurate, and prokaryotic species-specific predictor for identifying protein lysine acetylation sites.
- To address the limitations of current in silico prediction tools for Kace sites in prokaryotes.
Main Methods:
- Developed STALLION (STacking-based Predictor for ProkAryotic Lysine AcetyLatION) using a stacking strategy.
- Employed 11 encodings across three characteristics to extract patterns around Kace sites.
- Utilized rigorous feature selection and five tree-based ensemble algorithms to build species-specific baseline models.
Main Results:
- STALLION achieved high accuracy in identifying protein lysine acetylation sites.
- Comparative benchmarking demonstrated STALLION's superior performance over existing predictors on independent tests.
- A user-friendly online predictor for STALLION was implemented for accessibility.
Conclusions:
- STALLION represents a significant advancement in the accurate prediction of prokaryotic lysine acetylation sites.
- The developed predictor offers a valuable tool for researchers studying PTMs in prokaryotes.
- The online accessibility of STALLION facilitates broader application in biological research.
More Related Videos
07:26Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
Published on: December 26, 2020
12:49Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Related Concept Videos
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Ligand Binding and Linkage
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Conservation of Protein Domains