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Correlation between posttranslational modification and intrinsic disorder in protein.

ABSTRACT: Protein intrinsic disorder has been shown to play an important role in some posttranslational modifications (PTM). In this paper, we systematically investigated the correlation between protein disorder and dozens of PTMs using data from UniProt/Swiss-Prot and 3-D structures solved by NMR from Protein Data Bank. We observed that many PTMs have a preference for occurrence in disordered regions, including phospho-serine/-threonine/-tyrosine, hydroxylation, sulfotyrosine, S-geranylgeranyl cysteine, deamidated glutamine, 4-carboxyglutamate, 6'-bromotryptophan and most of methylation; while a few PTMs have a preference for occurrence in ordered regions, including 4-aspartylphosphate, S-nitrosocysteine, tele-methylhistidine, FMN conjugation, 4,5-dihydroxylysine, 3- methylthioaspartic acid, most of ADP-ribosylation, and most of FAD attachment. It is also noted that acetyllysine does not show any significant preference for occurrence in either disordered or ordered regions. Further analysis of NMR structures suggested disorder-toorder transitions might be introduced by modifications of phospho-serine/-threonine mono-/di-/tri-methyllysine, sulfotyrosine, 4-carboxyglutamate, and potentially 4-hydroxyproline. This study sheds light on the functions and mechanisms of various PTMs.

SUBMITTER: Gao J

PROVIDER: S-EPMC5120255 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Correlation between posttranslational modification and intrinsic disorder in protein.

Gao Jianjiong J Xu Dong D

Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing 20120101

Protein intrinsic disorder has been shown to play an important role in some posttranslational modifications (PTM). In this paper, we systematically investigated the correlation between protein disorder and dozens of PTMs using data from UniProt/Swiss-Prot and 3-D structures solved by NMR from Protein Data Bank. We observed that many PTMs have a preference for occurrence in disordered regions, including phospho-serine/-threonine/-tyrosine, hydroxylation, sulfotyrosine, S-geranylgeranyl cysteine, ...[more]

PMID: 22174266

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Project description:Cholesterol of the host macrophage membrane is vital for mycobacterial infection, replication, and persistence. During chronic infection within host lung tissues, cholesterol facilitates the phagocytosis of mycobacteria into macrophages. Cholesterol degradation leads to increased ﬂux of acetyl-coenzyme A (CoA) and propionyl-CoA, providing energy and building blocks for virulence macromolecules as well as donors for global protein acylation. Potential functions of lysine acylation are gradually revealed in bacterial survival and pathogenesis. However, the mycobacterial proteome and posttranslational modification (PTM) changes involved in the cholesterol catabolism bioprocess remain unclear. Here, we used nonpathogenic Mycobacterium smegmatis as a model and simultaneously monitored mycobacterial proteome and acetylome changes in the presence of glucose and cholesterol. We discovered that cholesterol metabolic enzymes were upregulated with respect to both protein expression levels and lysine acylation levels during the metabolic shift from glucose to cholesterol. After that, adenylating enzymes related to cholesterol metabolism were proven to be precisely regulated at the propionylation level by mycobacterial acyltransferase M. smegmatis Kat (MsKat) in response to cellular propionyl-CoA accumulation. Furthermore, the kinase expression and phosphorylation levels were also changed along with fluctuations in cholesterol levels. Our results expanded current knowledge of acylation regulation in the cholesterol catabolism of mycobacteria and provided references for possible antimycobacterium strategy.IMPORTANCE Cholesterol assimilation is a critical step in mycobacterial chronic infection. However, knowledge from the dynamic characterization of cholesterol metabolism in mycobacteria at the protein expression and PTM levels remains limited. Our study uncovered the landscape of protein expression, lysine acetylation, lysine propionylation, and S/T/Y phosphorylation during the metabolic changes from glucose to cholesterol in mycobacteria. The data showed that cholesterol-induced carbon shift resulted in the elevation of protein expression and lysine acylation in diverse metabolic enzymes involved in cholesterol degradation and that the presence of cholesterol also promoted the perturbations at the phosphorylation level in the kinase system in mycobacteria. This study systematically characterized the regulation of cholesterol catabolism at several different levels, which provided the detailed references in mycobacterial proteome and potential antimycobacterial strategies.

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Correlation between posttranslational modification and intrinsic disorder in protein.

Publications

Correlation between posttranslational modification and intrinsic disorder in protein.

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