RESUMO
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.
Assuntos
Acetilcoenzima A/química , Proteínas de Arabidopsis , Arabidopsis , Histona Acetiltransferases , Acetilação , Arabidopsis/enzimologia , Arabidopsis/genética , Proteínas de Arabidopsis/química , Proteínas de Arabidopsis/genética , Histona Acetiltransferases/química , Histona Acetiltransferases/genética , Domínios Proteicos , Análise de Sequência de ProteínaRESUMO
The study presents the results of bioinformatic comparison of protein phosphatases from higher plants and human phosphatom (150 sequences). Based on sequence and profile comparison with known catalytic domains, 204 plant homologues from Physcomitrella patens and Arabidopsis thaliana where selected. Clustering of joint group of plant and mammalian protein phosphatases revealed fundamental differences in plant and human phosphatomes. At the same time, it was shown significant differences in the set of protein phosphatases in P. patens, A. thaliana, and such monocots as Orysa saliva and Zea mays.
Assuntos
Arabidopsis/genética , Bryopsida/genética , Oryza/genética , Fosfoproteínas Fosfatases/genética , Proteínas de Plantas/genética , Zea mays/genética , Arabidopsis/classificação , Arabidopsis/enzimologia , Bryopsida/classificação , Bryopsida/enzimologia , Domínio Catalítico , Biologia Computacional , Humanos , Família Multigênica , Oryza/classificação , Oryza/enzimologia , Fosfoproteínas Fosfatases/química , Filogenia , Proteínas de Plantas/química , Homologia de Sequência de Aminoácidos , Especificidade da Espécie , Zea mays/classificação , Zea mays/enzimologiaRESUMO
The homology modeling, based on known temple structures of Homo sapiens protein phosphatase type-1 and -2A was implemented. The spatial structures of the human protein phosphatases and their plant homologs from Arabidopsis thaliana was predicted. The quality of models was confirmed by conformational analysis and root mean square deviations. The sites of okadaic acid binding in molecules of plant protein phosphatases (type-1 and -2A) were proved by the data of comparative analysis and molecular dynamics.
