The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes.

@article{Raghavan1992TheUO,
  title={The use of alternative substrates in the characterization of actin-methylating and carnosine-methylating enzymes.},
  author={Mala Raghavan and Uno Lindberg and Clarence Schutt},
  journal={European journal of biochemistry},
  year={1992},
  volume={210 1},
  pages={
          311-8
        }
}
Actin isolated from nearly every eukaryotic species contains approximately 1 mol 3-methylhistidine/mol protein. His73 in actin has been shown, by protein sequencing, to be the site of methylation. The methylation occurs enzymically and post-translationally. A rabbit skeletal muscle myofibrillary fraction has previously been shown to contain a histidine methyltransferase activity that is actin specific. Detailed study of this enzyme has been hampered by lack of a suitable substrate assay… Expand
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References

SHOWING 1-10 OF 29 REFERENCES
Partial purification and characterisation of S-adenosylmethionine:protein-histidine N-methyltransferase from rabbit skeletal muscle.
TLDR
A new class of protein methylase which methylates histidine residues of protein substrates using S-adenosylmethionine as the methyl donor has been partially purified from rabbit skeletal muscle, 22-fold with a yield of 56%. Expand
Analytical determination of methylated histidine in proteins: actin methylation.
TLDR
3-Methyl-histidine is the major methylation product in this in vitro reaction and is used in assays for the enzyme(s) responsible for methylation of rabbit skeletal muscle actin and to investigate the formation of other methylated residues in vitro. Expand
3-methylhistidine in actin and other muscle proteins.
TLDR
Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. Expand
Actin Amino-Acid Sequences
TLDR
The results obtained show that all three mammalian cytoplasmic actins studied contain the same amino-acid exchanges indicating that mammalian cy toplasmi actins are very similar if not identical in amino- acid sequence. Expand
Inhibition of purified p21 ras farnesyl:protein transferase by Cys-AAX tetrapeptides
TLDR
The enzyme was purified approximately 60,000-fold from rat brain cytosol through use of a chromatography step based on the enzyme's ability to bind to a hexapeptide containing the consensus sequence (Cys-AAX) for farnesylation. Expand
Pathways and the Physiological Site of Anserine Formation
TLDR
It is clear from in vivo1 and in vitro2 studies that vertebrate skeletal muscle contains an enzyme that can condense 1-methylhistidine and β-alanine to yield anserine, but it is not evident from such experiments whether N-methylation occurred at the histidine or carnosine stage, nor was the physiological site of anSerine formation revealed. Expand
In vitro synthesis of pp60v-src: myristylation in a cell-free system.
TLDR
The results imply that although myristate can be attached posttranslationally to synthetic peptide substrates, myristylation in vivo is apparently a very early cotranslational event which occurs before the first 100 amino acids of the nascent polypeptide chain are polymerized. Expand
Homologous methylated and nonmethylated histidine peptides in skeletal and cardiac myosins.
TLDR
It can be concluded that cardiac and skeletal myosin are synthesized under the control of different genes. Expand
Amino acid sequence of Acanthamoeba actin.
TLDR
By amino acid sequence studies, only one form of cytoplasmic actin was detected in Acanthamoeba castellanii, which is unique in containing a blocked NH2-terminal neutral amino acid (glycine), while all other actins sequenced thus far have a blocked acidic amino acid at the NH2 terminus. Expand
Actin of Naegleria gruberi. Absence of N tau-methylhistidine.
TLDR
This result indicates that N tau-methylhistidine is not a prerequisite for actin-actin or act in-myosin interactions, and raises questions about the function of multiple isoforms in a unicellular eukaryote. Expand
...
1
2
3
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