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Abundance of intrinsic structural disorder in the histone H1 subtypes

Paper ID Volume ID Publish Year Pages File Format Full-Text
14968 1365 2015 12 PDF Available
Title
Abundance of intrinsic structural disorder in the histone H1 subtypes
Abstract

•The disorder-promoting amino acids are dominant in the histones H1 sequences.•The disordered segments occur in all domains of histone H1 subtypes.•The histone H1 subtypes contain MoRFs and ANCHOR binding modules.•The histone H1 subtypes have widespread low-complexity regions and high folding rate.•The disorder is a permanent structural and functional feature of histone H1 subtypes.

The intrinsically disordered proteins consist of partially structured regions linked to the unstructured stretches, which consequently form the transient and dynamic conformational ensembles. They undergo disorder to order transition upon binding their partners. Intrinsic disorder is attributed to histones H1, perceived as assemblers of chromatin structure and the regulators of DNA and proteins activity. In this work, the comparison of intrinsic disorder abundance in the histone H1 subtypes was performed both by the analysis of their amino acid composition and by the prediction of disordered stretches, as well as by identifying molecular recognition features (MoRFs) and ANCHOR protein binding regions (APBR) that are responsible for recognition and binding. Both human and model organisms—animals, plants, fungi and protists—have H1 histone subtypes with the properties typical of disordered state. They possess a significantly higher content of hydrophilic and charged amino acid residues, arranged in the long regions, covering over half of the whole amino acid residues in chain. Almost complete disorder corresponds to histone H1 terminal domains, including MoRFs and ANCHOR. Those motifs were also identified in a more ordered histone H1 globular domain. Compared to the control (globular and fibrous) proteins, H1 histones demonstrate the increased folding rate and a higher proportion of low-complexity segments. The results of this work indicate that intrinsic disorder is an inherent structural property of histone H1 subtypes and it is essential for establishing a protein conformation which defines functional outcomes affecting on DNA- and/or partner protein-dependent cell processes.

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Keywords
Amino acid composition; ANCHOR protein binding regions; Folding rate; Intrinsic structural disorder; Histone H1 subtypes; Molecular recognition features
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Abundance of intrinsic structural disorder in the histone H1 subtypes
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Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 59, Part A, December 2015, Pages 16–27
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us