Author
RAO, R SHYAMA PRASAD - University Of Missouri | |
THELEN, JAY - University Of Missouri | |
Miernyk, Jan |
Submitted to: Trends in Plant Science
Publication Type: Review Article Publication Acceptance Date: 5/1/2014 Publication Date: 8/29/2014 Publication URL: http://handle.nal.usda.gov/10113/59549 Citation: Rao, R., Thelen, J.J., Miernyk, J.A. 2014. Is lys-Ne-acetylation the next big thing in post-translational modifications?. Trends in Plant Science. 19(9):550-553. Interpretive Summary: One important mechanism for modifying protein function involves a specific type of chemical modification whereby part of the protein is changed from being neutral to instead having a negative charge. An interacting three-part system is responsible for this chemical modification. Recently, a second type of chemical modification has been described in animal cells and microbes. This second chemical modification changes part of the protein from having a positive charge to being neutral. This second system of chemical modification is also mediated by a three-part system. We describe the occurrence of this second chemical modification system in plant cells, and compare it with the systems in animal cells and microorganisms. This information will be important for researchers who study control of protein function, and to those using a biotechnology-based approach to modify crop plants. Technical Abstract: Lys-N'-acetylation (KAC) has recently ascended from a posttranslational modification (PTM) of limited distribution to one approaching the abundance of O-phosphorylation. Thousands of KAC-proteins have been identified in archaea, bacteria, and eukarya, and the KAC system of acetyltransferases, deacetylases, and binding-proteins is superficially comparable with the kinases, phosphatases, and P-protein binding-proteins of O-phosphorylation. Herein we describe recent results, and compare several aspects of these two major systems of PTM in plants. |