Linked Life Data

7318833

Source:http://linkedlifedata.com/resource/pubmed/id/7318833

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-3-22
pubmed:abstractText
The class of lysine-rich histones, H1, found in most eukaryotic cells is largely replaced by another class of lysine-rich histones, H5, in avian and other erythrocytes. Erythrocytes are transcriptionally inert and this state has been attributed to the presence of H5. Although there are many sequence differences between H1 and H5 both molecules have very similar structures with three well-defined domains: a flexible basic N-terminal region, an apolar globular central region and a flexible basic C-terminal region. The lengths of the N-terminal regions are different for H1 and H5 whereas the lengths of the central and C-terminal regions are very similar. Considerable interest attaches to the findings that another type of mammalian lysine-rich histone H1(0) has an apolar region exhibiting considerable sequence homology (70%) with the central globular region of H5. The abundance of H1 in cells has been found to correlate inversely with their mitotic activities. Conformational studies using high-resolution nuclear magnetic resonance and optical spectroscopy have been made of H1 and its conformational behaviour has been compared with those of H1 and H5. H1 has been found to contain a central globular region of similar size to those found in H1 and H5. However, the conformation and stability of the globular domain of H1 are very similar to the globular region of H5 rather than H1. H1 appears to be a hybrid containing a major feature of the H5 histone. The globular regions of H1 and H5 are known to bind to a specific site on the nucleosome sealing off two turns of DNA. It is proposed that H1 binds to the same site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
120
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Conformation studies of histone H1(0) in comparison with histones H1 and H5.
pubmed:publicationType
Journal Article, Comparative Study