In vitro Methylation of Muscle Proteins

3-METHYL HISTIDINE is a normal amino-acid component of myosin from adult muscle 1 and of actin 1,2 . But whereas 3-methyl histidine occurs in actin isolated from adult and foetal muscle it is absent from myosin isolated from skeletal muscle of the foetal rabbit. After birth the amount of this amino-...

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Bibliographic Details
Published in:Nature (London) 1969-07, Vol.223 (5203), p.300-302
Main Authors: HARDY, MADELEINE F, PERRY, S. V
Format: Article
Language:English
Subjects:
Animals
Animals, Newborn
Autoradiography
Carbon Isotopes
Chromatography
Electrophoresis
Histidine - analysis
Humanities and Social Sciences
In Vitro Techniques
letter
Methionine
Methylation
multidisciplinary
Muscle Proteins
Rabbits
Science
Science (multidisciplinary)
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Summary:3-METHYL HISTIDINE is a normal amino-acid component of myosin from adult muscle 1 and of actin 1,2 . But whereas 3-methyl histidine occurs in actin isolated from adult and foetal muscle it is absent from myosin isolated from skeletal muscle of the foetal rabbit. After birth the amount of this amino-acid in myosin from rabbit skeletal muscle increases until it reaches the adult value 3 . This implies that development in muscle is accompanied by the methylation of histidine residues of myosin. Nothing is known of the mechanism of this process and, although it has not been directly demonstrated that the methyl group of methionine is a precursor of the methyl group of 3-methyl histidine found in actin, the results of Asatoor and Armstrong 2 , obtained with whole animals, are compatible with such a mechanism. We have studied in vitro the methylation of muscle proteins with S-adenosyl methionine labelled with 14 C in the methyl group in an attempt to elucidate the mechanism of formation of the 3-methyl histidine present in myosin and actin.
ISSN:0028-0836
1476-4687
DOI:10.1038/223300a0