Related Experiment Video
Updated: Aug 9, 2026

08:57
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
A highly conserved 3-methylhistidine modification is absent in yeast actin
H R Kalhor1, A Niewmierzycka, K F Faull
1Department of Chemistry, University of California, Los Angeles, California, 90095, USA.
Archives of Biochemistry and Biophysics
|September 25, 1999
Summary
Researchers investigated protein histidine methyltransferase in yeast actin, finding histidine-73 is unexpectedly unmodified in Saccharomyces cerevisiae and Candida albicans, unlike rabbit actin. This suggests the methylation evolved later in higher eukaryotes.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Protein methylation, specifically histidine methylation, is a crucial post-translational modification.
- 3-methylhistidine (3-MeHis) is a conserved residue in actin across many species.
- The presence and function of protein histidine methyltransferases (PHMTs) in yeast are not fully understood.
Purpose of the Study:
- To identify a PHMT in Saccharomyces cerevisiae by examining actin modification.
- To determine if the conserved histidine at position 73 (His-73) in yeast actin is methylated.
- To compare histidine methylation patterns in yeast actin with other eukaryotic actins.
Main Methods:
- Amino acid analysis of purified actin from Saccharomyces cerevisiae and Candida albicans.
- Tryptic digestion of actin followed by amino acid analysis and mass spectrometry.
- Phylogenetic analysis of actin sequences from various eukaryotic organisms.
Main Results:
- Histidine-73 in Saccharomyces cerevisiae actin is not modified with 3-methylhistidine.
- Actin from Candida albicans also lacks modification at His-73.
- Rabbit muscle actin contains the expected 3-methylhistidine residue.
- Phylogenetic analysis indicates 3-MeHis modification in actin evolved after yeast divergence from higher eukaryotes.
Conclusions:
- The identified methodology provides an improved approach for analyzing histidine methylation in proteins.
- The absence of 3-MeHis at His-73 in yeast suggests a loss or late acquisition of this specific methylation event in eukaryotic evolution.
- Further research is needed to identify the specific PHMTs responsible for actin methylation in higher eukaryotes.
Related Concept Videos
Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
Introduction to Actin
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across different species.
Heterochromatin
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Actin Polymerization and Cell Motility
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Histone Modification
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

