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Discovering Relationships Between Lysine Ubiquitylation and Acetylation Sites from Proteomic Datasets
Author(s) -
Elwood Jake,
Maki Jennifer,
Freund Dana
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.567.17
Subject(s) - lysine , acetylation , proteomics , biochemistry , ubiquitin , computational biology , arabidopsis thaliana , proteasome , protein degradation , chemistry , posttranslational modification , arabidopsis , biology , enzyme , amino acid , mutant , gene
Ubiquitylation (Ub) and acetylation (Ac) are post translational modifications that both occur on lysine residues. Ac of non‐nuclear proteins is a new area of research, especially in the plant biology field. Ac of proteins can alter enzyme activities and protein functions, while Ub is well known for marking proteins for degradation by the proteasome as well as many other cellular functions. Recently, it has been suggested that competition may exist between Ub and Ac of specific lysine residues. It may be that the neutralization of the lysine side chain caused by Ac prevents Ub from taking place. If proven, this Ac‐Ub competition has the potential to affect processes such as the regulation of the cell cycle and protein degradation. The purpose of this study was to manually data mine previously published Ac and Ub sites in Arabidopsis thaliana to determine the amount of overlap. Sites identified in three publications were compared: Finkemeier et al (2011) Plant Physiol, 155:1779‐90; Kim et al (2013) The Plant Cell, 25: 1523‐40; and Wu et al (2011) Plant Physiol, 155:1769‐78. Thus far, seven of the modified proteins are subjected to both of these post‐translational modifications. Further analysis has been initiated to locate the specific Ub lysine residues and compare sites to known Ac lysine sites of the same protein. Currently, more extensive mass spectrometry based proteomics studies are underway to expand the number of identified Ac sites. Future work will investigate other plant species and other types of acylations. This project is part of a collaboration between The College of St. Scholastica and The University of Minnesota and provides research opportunities for undergraduates.