EurekaMag.com logo
+ Site Statistics
References:
53,517,315
Abstracts:
29,339,501
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Regions of intrinsic disorder help identify a novel nuclear localization signal in Toxoplasma gondii histone acetyltransferase TgGCN5-B



Regions of intrinsic disorder help identify a novel nuclear localization signal in Toxoplasma gondii histone acetyltransferase TgGCN5-B



Molecular and Biochemical Parasitology 175(2): 192-195



We have previously shown that protozoan parasites, such as Toxoplasma gondii, contain a high prevalence of intrinsically disordered regions in their predicted proteins. Here, we determine that both TgGCN5-family histone acetyltransferases (HATs) contain unusually high levels of intrinsic disorder. A previously identified basic-rich nuclear localization signal (NLS) in the N-terminus of TgGCN5-A is located within such a region of predicted disorder, but this NLS is not conserved in TgGCN5-B. We therefore analyzed the intrinsically disordered regions of TgGCN5-B for basic-rich sequences that could be indicative of a functional NLS, and this led to the identification of a novel NLS for TgGCN5-B, RPAENKKRGR. The functionality of the GCN5-B NLS was validated experimentally and has predictive value. These studies demonstrate that basic-rich sequences within regions predicted to be intrinsically disordered constitute criteria for a candidate NLS.

(PDF same-day service: $19.90)

Accession: 055445438

Download citation: RISBibTeXText

PMID: 21055425

DOI: 10.1016/j.molbiopara.2010.10.009



Related references

Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites. Nucleic Acids Research 27(22): 4344-4352, 1999

Quinoline derivative MC1626, a putative GCN5 histone acetyltransferase (HAT) inhibitor, exhibits HAT-independent activity against Toxoplasma gondii. Antimicrobial Agents and ChemoTherapy 51(3): 1109-1111, 2006

Cloning and characterization of a novel histone acetyltransferase homologue from the protozoan parasite Toxoplasma gondii reveals a distinct GCN5 family member. Gene 242(1/2): 193-200, 2000

Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii. Molecular Biosystems 9(4): 645-657, 2013

Canonical histone H2Ba and H2A.X dimerize in an opposite genomic localization to H2A.Z/H2B.Z dimers in Toxoplasma gondii. Molecular and Biochemical Parasitology 197(1-2): 36-42, 2015

Mitochondrial localization of non-histone protein HMGB1 during human endothelial cell-Toxoplasma gondii infection. Cell Biology International 32(2): 235-238, 2007

Toxoplasma gondii Hsp70 as a danger signal in toxoplasma gondii-infected mice. Cell Stress & Chaperones 5(4): 328-335, 2000

Role of Toxoplasma gondii HSP70 and Toxoplasma gondii HSP30/bag1 in antibody formation and prophylactic immunity in mice experimentally infected with Toxoplasma gondii. Microbiology and Immunology 43(5): 471-479, 1999

Nuclear import of histone deacetylase 5 by requisite nuclear localization signal phosphorylation. Molecular & Cellular Proteomics 10(2): M110.004317-M110.004317, 2011

Identification of a novel nuclear localization signal common to 69- and 82-kDa human choline acetyltransferase. Journal of Biological Chemistry 278(22): 20217-20224, 2003

Identification of a novel nuclear localization signal in cytoplasmic 69 kDa human choline acetyltransferase. Molecular Biology of the Cell 13(Supplement): 525a, 2002

Opposite responses of nuclear spermidine N8-acetyltransferase and histone acetyltransferase activities to regenerative stimuli in rat liver. Hepatology 15(5): 928-933, 1992

Calf liver nuclear N-acetyltransferases. Purification and properties of two enzymes with both spermidine acetyltransferase and histone acetyltransferase activities. Journal of Biological Chemistry 253(1): 233-237, 1978