Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/430
Title: Prediction of an HMG-Box Fold in the C-Terminal Domain of Histone H1: Insights Into Its Role in DNACondensation
Authors: Bharath, M M S
Chandra, Nagasuma R
Rao, M R S
Keywords: HMG-box fold
histone H1
DNA condensation
C-terminal domain
chromatin organization
Issue Date: Oct-2002
Publisher: Wiley-Liss Inc
Citation: Protiens: Structure, Function, and Genetics 49(1), 71–81 (2002)
Abstract: In eukaryotes, histone H1 promotes the organization of polynucleosome filaments into chromatin fibers, thus contributing to the formation of an important structural framework responsible for various DNA transaction processes. The H1 protein consists of a short N-terminal "nose," a central globular domain, and a highly basic C-terminal domain. Structure prediction of the C-terminal domain using fold recognition methods reveals the presence of an HMG-box-like fold. We recently showed by extensive site-directed and deletion mutagenesis studies that a 34 amino acid segment encompassing the three S/TPKK motifs, within the C-terminal domain, is responsible for DNA condensing properties of H1. The position of these motifs in the predicted structure corresponds exactly to the DNA-binding segments of HMG-box-containing proteins such as Lef-1 and SRY. Previous analyses have suggested that histone H1 is likely to bend DNA bound to the C-terminal domain, directing the path of linker DNA in chromatin. Prediction of the structure of this domain provides a framework for understanding the higher order of chromatin organization.
Description: Restricted Access
URI: http://hdl.handle.net/10572/430
Other Identifiers: 1097-0134
Appears in Collections:Research Papers (M.R.S. Rao)

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