Linked Life Data

15465822

Source:http://linkedlifedata.com/resource/pubmed/id/15465822

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
53
pubmed:dateCreated
2004-12-23
pubmed:abstractText
Although it has been proposed that the secondary bile acids, deoxycholic acid and lithocholic acid, increase the number of aberrant crypt foci in the colon and may act as colon tumor promoters, there is little evidence detailing their mechanism of action. Histones play an important role in controlling gene expression, and the posttranslational modification of histones plays a role in regulation of intracellular signal transduction. In particular, the amino-terminal tail domain of histone H3 is sensitive to several posttranslational modifications, and acetylation of this domain changes its electrostatic environment and results in the loss of native folding. Therefore, we studied the modification of epsilon-amino groups on human histone H3 by deoxycholyl adenylate, which is an active intermediate in deoxycholyl thioester biosynthesis. After incubation of recombinant human histone H3 with a smaller amount of acyl adenylate, followed by enzymatic digestion, the peptide fragment mixtures were analyzed by matrix-assisted laser desorption ionization mass spectrometry. These data showed the formation of only one adduct fragment, which corresponded to amino acids 3-8 with a deoxycholate adduct, suggesting that the epsilon-amino group of Lys(4) had the highest reactivity. This novel modification, formation of a bile acid adduct on the histone H3 amino-terminal tail domain through an active acyl adenylate, may relate to the carcinogenesis-promoting effects of secondary bile acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
55034-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15465822-Amino Acid Sequence, pubmed-meshheading:15465822-Bile Acids and Salts, pubmed-meshheading:15465822-Chromatography, High Pressure Liquid, pubmed-meshheading:15465822-DNA Adducts, pubmed-meshheading:15465822-Deoxycholic Acid, pubmed-meshheading:15465822-Histones, pubmed-meshheading:15465822-Humans, pubmed-meshheading:15465822-Ions, pubmed-meshheading:15465822-Lysine, pubmed-meshheading:15465822-Models, Chemical, pubmed-meshheading:15465822-Models, Molecular, pubmed-meshheading:15465822-Molecular Sequence Data, pubmed-meshheading:15465822-Protein Structure, Tertiary, pubmed-meshheading:15465822-Recombinant Proteins, pubmed-meshheading:15465822-Signal Transduction, pubmed-meshheading:15465822-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:15465822-Temperature
pubmed:year
2004
pubmed:articleTitle
A nonenzymatic modification of the amino-terminal domain of histone H3 by bile acid acyl adenylate.
pubmed:affiliation
Graduate School of Pharmaceutical Sciences, Tohoku University, 101 Seiryo-machi, Aobayama, Aoba-ku, Sendai 980-8578, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't