title: 3D structure prediction of histone acetyltransferase proteins of the MYST family and their interactome in Arabidopsis thaliana.
abstract: Histone lysine acetylation is a reversible post-translational modification that does not involve changes in DNA sequences. Enzymes play an important role in developmental processes and their deregulation has been linked to the progression of diverse disorders. The HAT enzyme family fulfills an important role in various developmental processes mediated by the state of chromatin, and have been attributed to its deregulation. To understand acetylation mechanisms and their role in cell signaling, transcriptional regulation, and apoptosis, it is crucial to identify and analyze acetylation sites. Bioinformatics methods can be used to generate relatively precise predictions. Here we applied classical bioinformatics methods-sequence alignment, homology modeling, and docking-to compare approved and predicted lysine acetylation processes in different organisms. HAM1 and HAM2 are analogs of KAT8 and KAT7 (MYST1 and MYST2), members of the MYST histone acetyltransferase family, and our results show that HAM1 and HAM2 have much in common with other representatives of MYST families from various organisms. One function of acetyl-CoA binding was predicted with a high level of probability by computational methods. Based on our data, we conclude that, despite huge genetic distances and some structural differences between animal and plant species, a closer look at acetylation mechanism shows that they have much in common.
authors.affiliation: Laboratory of Structural Biology, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine. rayevsky85@gmail.com.
authors.forename: A V
authors.initials: AV
authors.lastname: Raevsky
authors.affiliation: Medway School of Pharmacy, Universities of Kent and Greenwich, Chatham, Kent, ME4 4TB, UK.|Division of Systems Biology, National Center for Toxicological Research, US Food and Drug Administration, Jefferson, AR, USA.
authors.forename: M
authors.initials: M
authors.lastname: Sharifi
authors.affiliation: Laboratory of Structural Biology, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine.
authors.forename: D A
authors.initials: DA
authors.lastname: Samofalova
authors.affiliation: Laboratory of Structural Biology, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine.
authors.forename: P A
authors.initials: PA
authors.lastname: Karpov
authors.affiliation: Laboratory of Structural Biology, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, 04123, Kyiv, Ukraine.
authors.forename: Y B
authors.initials: YB
authors.lastname: Blume
mesh_terms: D000105:Acetyl Coenzyme A / Q000737:chemistry*; D000107:Acetylation; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000235:genetics; D000072417:Protein Domains; D020539:Sequence Analysis, Protein
chemical_list: D029681:Arabidopsis Proteins; D000105:Acetyl Coenzyme A; D051548:Histone Acetyltransferases
keywords: Arabidopsis thaliana; HAM1/HAM2; Histone acetylation; MYST