Related Experiment Video
Updated: Jul 20, 2026

11:44
Primary Culture of Adult Rat Heart Myocytes
Published on: June 16, 2009
Structure of a gene for rat calmodulin.
Journal of Molecular Biology
|February 5, 1987
Summary
Researchers elucidated the rat calmodulin gene structure, revealing six exons and variable introns. Key intron/exon junctions align with calcium-binding subdomains and chicken calmodulin, offering insights into gene regulation.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Calmodulin is a crucial calcium-binding protein involved in numerous cellular processes.
- Understanding the gene structure provides insights into gene regulation and evolution.
Purpose of the Study:
- To determine the complete structural organization of the rat calmodulin gene.
- To identify intron/exon boundaries and regulatory elements within the gene.
Main Methods:
- Cloning and sequencing of overlapping genomic and cDNA clones from rat genomic and brain libraries.
- Direct comparison of genomic and cDNA sequences to map intron/exon organization.
- Analysis of the 5' upstream region for regulatory sequences.
Main Results:
- The rat calmodulin gene spans 9000 bases, comprising six exons separated by introns.
- Intron/exon junctions within coding regions are located in calcium-binding subdomains, similar to chicken calmodulin.
- A repetitive sequence homologous to a rat identifier sequence was found in the third intron.
- The 5' upstream region contains a TATA box and C-G boxes, but not a CAT box.
- A conserved sequence was identified upstream of both rat and chicken calmodulin genes.
Conclusions:
- The structural organization of the rat calmodulin gene, including intron/exon positioning, is conserved with chicken calmodulin.
- The identified regulatory elements suggest specific transcriptional control mechanisms.
- The presence of repetitive sequences may play a role in gene regulation or evolution.
Related Concept Videos
Cell Specific Gene Expression
Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
Master Transcription Regulators
Master transcription regulators are regulatory proteins that are predominantly responsible for regulating the expression of multiple genes. Often these genes work in concert to drive a complex process. Activation of a master transcription regulator can lead to a cascade of transcriptional activation necessary for that outcome. These regulators can directly bind to the regulatory sequences of the various genes involved, or they can indirectly regulate transcription by binding to regulatory...
Cis-regulatory Sequences
Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
Activation and Inactivation of G Proteins
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Structure of Cadherins
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

