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. 2011 Jul 12:6:15.
doi: 10.1186/1747-1028-6-15.

Human linker histones: interplay between phosphorylation and O-β-GlcNAc to mediate chromatin structural modifications

Waqar Ahmad  1 , Khadija Shabbiri, Noreen Nazar, Shazia Nazar, Saba Qaiser, Mirza Abid Shabbir Mughal
Affiliations

Human linker histones: interplay between phosphorylation and O-β-GlcNAc to mediate chromatin structural modifications

Waqar Ahmad et al. Cell Div. .

Abstract

Eukaryotic chromatin is a combination of DNA and histone proteins. It is established fact that epigenetic mechanisms are associated with DNA and histones. Initial studies emphasize on core histones association with DNA, however later studies prove the importance of linker histone H1 epigenetic. There are many types of linker histone H1 found in mammals. These subtypes are cell specific and their amount in different types of cells varies as the cell functions. Many types of post-translational modifications which occur on different residues in each subtype of linker histone H1 induce conformational changes and allow the different subtypes of linker histone H1 to interact with chromatin at different stages during cell cycle which results in the regulation of transcription and gene expression. Proposed O-glycosylation of linker histone H1 promotes condensation of chromatin while phosphorylation of linker histone H1 is known to activate transcription and gene regulation by decondensation of chromatin. Interplay between phosphorylation and O-β-GlcNAc modification on Ser and Thr residues in each subtype of linker histone H1 in Homo sapiens during cell cycle may result in diverse functional regulation of proteins. This in silico study describes the potential phosphorylation, o-glycosylation and their possible interplay sites on conserved Ser/Thr residues in various subtypes of linker histone H1 in Homo sapiens.

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Figures

Figure 1
Figure 1
Sequence alignment of different subtypes of linker histone H1 present in Homo sapiens. The residues highlighted in red show conserved and conserved substitution regions in Ser and Thr residues, while the regions highlighted in yellow show that Ser and Thr residues which are conserved in maximum subtypes but not present in all of the subtypes in linker histone H1. The consensus sequences (motifs) for phosphorylation are shown in square lines.
Figure 2
Figure 2
Graphical presentation of potential for phosphate modification at Ser, Thr and Tyr residues in different subtypes of linker histone H1 in Homo sapiens. Here blue vertical line show the phosphorylation potential of Ser, green vertical lines show the phosphorylation potential of Thr residues, redlines show phosphorylation potential of Tyr residues, and gray horizontal lines show threshold for modification potential in each subtype of linker histone H1.
Figure 3
Figure 3
Graphical representation of potential for O-β-GlcNAc modification in Ser and Thr residues in the different subtypes of linker histone H1 in Homo sapiens. Green vertical lines show the potential of Ser/Thr residues for O-β-GlcNAc modification and light blue horizontal wavy lines show threshold for modification potential.
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