Related Experiment Video
Updated: Apr 29, 2026

08:57
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
7.8K
Multiple, heterogeneous actin genes in Dictyostelium
Cell
|November 1, 1978
Summary
Researchers identified a new plasmid, pDd actin 2, containing two actin genes. These genes show significant homology, suggesting a conserved functional region essential for actin protein coding.
Area of Science:
- Molecular Biology
- Genetics
Background:
- Actin genes are crucial for cellular structure and function.
- Previous studies identified actin genes in plasmids like M6, pcDd actin B1, and pcDd actin A1.
Purpose of the Study:
- To characterize a newly identified actin gene-containing plasmid, pDd actin 2.
- To investigate the homology and divergence between different actin genes.
Main Methods:
- Plasmid selection using restriction fragments.
- Heteroduplex formation to assess gene homology.
- Thermal denaturation experiments to determine gene divergence.
- Agarose gel electrophoresis to analyze mRNA size classes.
Main Results:
- Plasmid pDd actin 2 contains two actin genes separated by 350 bp of nonactin DNA.
- A conserved homology region of 1100 +/- 100 bp was identified between actin genes.
- Actin gene pairs diverged by 6-8% based on thermal denaturation.
- Two mRNA size classes (1.25 kb and 1.35 kb) complementary to the actin genes were observed.
Conclusions:
- The identified homology region is close to the minimum length required for actin protein coding.
- The findings provide insights into the structure and evolution of actin gene families.
- Further investigation into the linkage of these actin genes is warranted.
Related Concept Videos
Introduction to Actin
4.6K
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...
4.6K
Actin Polymerization
6.3K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
6.3K
Generation of Straight or Branched Actin Filaments
2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K
Actin Filament Depolymerization
3.0K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
3.0K
Formation of Higher-order Actin Filaments
2.8K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
2.8K
Actin Polymerization and Cell Motility
5.8K
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....
5.8K

