Document Detail


Characterization of sequence variations in human histone H1.2 and H1.4 subtypes.
MedLine Citation:
PMID:  16008566     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In humans, eight types of histone H1 exist (H1.1-H1.5, H1 degrees , H1t and H1oo), all consisting of a highly conserved globular domain and less conserved N- and C-terminal tails. Although the precise functions of these isoforms are not yet understood, and H1 subtypes have been found to be dispensable for mammalian development, it is now clear that specific functions may be assigned to certain individual H1 subtypes. Moreover, microsequence variations within the isoforms, such as polymorphisms or mutations, may have biological significance because of the high degree of sequence conservation of these proteins. This study used a hydrophilic interaction liquid chromatographic method to detect sequence variants within the subtypes. Two deviations from wild-type H1 sequences were found. In K562 erythroleukemic cells, alanine at position 17 in H1.2 was replaced by valine, and, in Raji B lymphoblastoid cells, lysine at position 173 in H1.4 was replaced by arginine. We confirmed these findings by DNA sequencing of the corresponding gene segments. In K562 cells, a homozygous GCC-->GTC shift was found at codon 18, giving rise to H1.2 Ala17Val because the initial methionine is removed in H1 histones. Raji cells showed a heterozygous AAA-->AGA codon change at position 174 in H1.4, corresponding to the Lys173Arg substitution. The allele frequency of these sequence variants in a normal Swedish population was found to be 6.8% for the H1.2 GCC-->GTC shift, indicating that this is a relatively frequent polymorphism. The AAA-->AGA codon change in H1.4 was detected only in Raji cells and was not present in a normal population or in six other cell lines derived from individuals suffering from Burkitt's lymphoma. The significance of these sequence variants is unclear, but increasing evidence indicates that minor sequence variations in linker histones may change their binding characteristics, influence chromatin remodeling, and specifically affect important cellular functions.
Authors:
Bettina Sarg; Anna Gréen; Peter Söderkvist; Wilfried Helliger; Ingemar Rundquist; Herbert H Lindner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The FEBS journal     Volume:  272     ISSN:  1742-464X     ISO Abbreviation:  FEBS J.     Publication Date:  2005 Jul 
Date Detail:
Created Date:  2005-07-12     Completed Date:  2005-09-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  3673-83     Citation Subset:  IM    
Affiliation:
Division of Clinical Biochemistry, Biocenter, Innsbruck Medical University, Austria.
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MeSH Terms
Descriptor/Qualifier:
Base Sequence
Cell Line
Chromatography, High Pressure Liquid
Histones / classification*,  genetics*
Humans
Hydrophobicity
Polymorphism, Genetic / genetics*
Chemical
Reg. No./Substance:
0/Histones

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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