Cytochrome c-specific protein methylase III from Neurospora crassa

A protein methylase III responsible for specifically methylating the cytochrome c in Neurospora crassa was partially characterized by using unmethylated horse heart cytochrome c as a substrate. This enzyme utilizes S-adenosyl-L-methionine as the methyl donor. An analysis of the distribution of [14C]...

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Bibliographic Details
Published in:Biochemical journal 1977-07, Vol.165 (1), p.11-18
Main Authors: Nochumson, S, Durban, E, Kim, S, Paik, W K
Format: Article
Language:English
Subjects:
Chymotrypsin - pharmacology
Cytochrome c Group
Histone-Lysine N-Methyltransferase - analysis
Histone-Lysine N-Methyltransferase - isolation & purification
Kinetics
Lysine - pharmacology
Methylation
Neurospora - enzymology
Neurospora crassa - enzymology
Protein Methyltransferases - analysis
Subcellular Fractions - enzymology
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Summary:A protein methylase III responsible for specifically methylating the cytochrome c in Neurospora crassa was partially characterized by using unmethylated horse heart cytochrome c as a substrate. This enzyme utilizes S-adenosyl-L-methionine as the methyl donor. An analysis of the distribution of [14C]methyl groups in the peptides obtained by chymotrypsin digestion of the enzymically methylated cytochrome c showed that all of the radioactivity could be recovered within a single peak after chromatography. This indicates that the enzyme methylates a specific amino acid sequence within cytochrome c. On hydrolysis of the radioactive chymotryptic peptide, Me-14C-labelled epsilon -N-mono-methyl-lysine, epsilon-N-dimethyl-lysine and epsilon-N-trimethyl-lysine were identified. The enzyme can easily be extracted from the N. crassa mycelial pads and was purified approx. 30-fold.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1650011