Histone biotinylation in Candida albicans
Sahar Hasim1, Swetha Tati, Nandakumar Madayiputhiya
1School of Biological Sciences, University of Nebraska, Lincoln, NE, USA.
FEMS Yeast Research
|May 31, 2013
Summary
Biotin modifies histones in Candida albicans, a human fungal pathogen. This histone biotinylation was observed in biotin-replete cells but not in Saccharomyces cerevisiae, suggesting a potential role in biotin storage.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- * Candida albicans is an opportunistic human fungal pathogen known for its polymorphism.
- * Biotin is an essential cofactor for carboxylases involved in cell growth and fatty acid metabolism.
- * Histone modifications play crucial roles in regulating gene expression and chromatin structure.
Purpose of the Study:
- * To investigate the role of biotin in Candida albicans beyond its known metabolic functions.
- * To determine if biotin is involved in post-translational modification of histones in C. albicans.
- * To characterize the nature and extent of histone biotinylation.
Main Methods:
- * Detection of biotinylation using Western blots with an antibiotin antibody.
- * Mass spectrometry techniques (qTOF and LC/MS/MS) for identifying biotinylated histones.
- * Comparison of histone modifications in biotin-replete versus biotin-starved C. albicans cells.
Main Results:
- * Histone biotinylation was detected in C. albicans, specifically modifying histones H2A, H2B, and H4 at multiple lysine residues.
- * Biotinylation occurred in a non-site-specific manner and was dependent on biotin availability, observed only in biotin-replete cells.
- * Other common histone modifications (acetylation, methylation, phosphorylation) were present at similar levels in both replete and starved cells, indicating biotinylation is distinct.
- * No histone biotinylation was detected in Saccharomyces cerevisiae using the same methods.
Conclusions:
- * Biotinylation of histones represents a novel post-translational modification in Candida albicans.
- * The observed histone biotinylation is specific to C. albicans and dependent on biotin availability.
- * While the precise function remains unknown, histone biotinylation may serve as a biotin storage mechanism in C. albicans, which is a natural biotin auxotroph.
More Related Videos
Related Concept Videos
02:30Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:25Spreading of Chromatin Modifications
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer is an enzyme that can...
Writers
The writer is an enzyme that can...