Methylation-like reaction of [3H-methyl]-N-5-trimethyllysine (TML) to chromatin components

A. Jeney, G. Gyapay, K. Lapis

Research output: Contribution to journalArticle

Abstract

To elucidate the mechanism of action of N-5-trimethyllysine, an endogenous amino acid derivative with stimulatory action on cell proliferation, the binding of [3H-CH3]-N-5-trimethyllysine (TML) to DNA, histones and non-histones was investigated in NK/Ly ascites tumour cells. Radioactivity was detected in all of the chromatin components, particularly in the non-histone fractions. Chromatin proteins separated on polyacrylamide gel electrophoresis revealed the preferential binding of TML to histones H1 and H4, and also to two groups of non-histones with molecular weights around 60 X 103 and 12 X 103 daltons. The binding of TML to DNA was mainly associated with adenine and in a purified nuclei assay system could be increased by manganese and inhibited by magnesium.

Original languageEnglish
Pages (from-to)2729-2732
Number of pages4
JournalBiochemical Pharmacology
Volume29
Issue number20
DOIs
Publication statusPublished - 1980

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Methylation
Chromatin
Histones
DNA
Radioactivity
Cell proliferation
Adenine
Manganese
Electrophoresis
Ascites
Magnesium
Tumors
Polyacrylamide Gel Electrophoresis
Assays
Molecular Weight
Molecular weight
Cells
Cell Proliferation
Derivatives
Amino Acids

ASJC Scopus subject areas

  • Pharmacology

Cite this

Methylation-like reaction of [3H-methyl]-N-5-trimethyllysine (TML) to chromatin components. / Jeney, A.; Gyapay, G.; Lapis, K.

In: Biochemical Pharmacology, Vol. 29, No. 20, 1980, p. 2729-2732.

Research output: Contribution to journalArticle

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