Analysis of the effects of the methyltransferase encoded by Rv3263 on gene expression in M. tuberculosis
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ABSTRACT:
ORGANISM(S): Mycobacterium tuberculosis H37Rv
SUBMITTER: Scarlet Shell
PROVIDER: E-GEOD-46432 | biostudies-arrayexpress |
REPOSITORIES: biostudies-arrayexpress
Similar Datasets
Project description:DNA methylation affects gene expression in many organisms. To determine to effects of DNA methylation on gene expression in M. tuberculosis, we genetically deleted a predicted DNA methyltransferase encoded by Rv3263 and subjected wildtype, mutant, and complemented strains to global expression analysis.
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Project description:Total protein and membrane-enriched fractions of Synechocystis sp. PCC 6803 wild type (WT) and mutant strains affected with inactivated DNA methyltransferase genes were analyzed by LC-HDMSE. The mutation of the DNA methyltransferase gene sll0729 encoding M.Ssp6803II initially led to a strong phenotype, including a lowered chlorophyll/phycocyanin ratio, impaired growth, and alterations in gene expression. Prolonged cultivation revealed instability of the initially obtained phenotype. Colonies showing normal pigmentation and WT-like growth appeared regularly and in high frequencies on agar plates. These colonies represent suppressor mutants, since the sll0729 gene is still completely inactivated and methylation of the M.Ssp6803II target GGCC sites does not occur. The proteomic analysis comprises the WT, two strains of suppressor mutants sll0729_1 and sll0729_15 as well as mutants of the DNA methyltransferase genes slr6095 and sll8009. For each of these five strains we investigated three biological replicates. Comparisons between the WT and these two suppressor mutant strains, but also between them and the slr6095 and sll8009 mutants enabled the detection of expression differences, which are specifically linked to the absence of M.Ssp6803II-related DNA methylation.
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Project description:The DNA methyltransferase activity of DNMT1 is vital for genomic maintenance of DNA methylation. We report here that DNMT1 function is regulated by O-GlcNAcylation, a protein modification that is sensitive to glucose levels, and that elevated O-GlcNAcylation of DNMT1 from high glucose environment leads to alterations to the epigenome. Using mass spectrometry and complementary alanine mutation experiments, we identified S878 as the major residue that is O-GlcNAcylated on DNMT1. Functional studies further revealed that O-GlcNAcylation of DNMT1-S878 results in an inhibition of methyltransferase activity, resulting in a general loss of DNA methylation that is preferentially at partially methylated domains (PMDs). This loss of methylation corresponds with an increase in DNA damage and apoptosis. These results establish O-GlcNAcylation of DNMT1 as a mechanism through which the epigenome is regulated by glucose metabolism and implicates a role for glycosylation of DNMT1 in metabolic diseases characterized by hyperglycemia.
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