Related Experiment Video
Updated: Jul 17, 2026

12:03
Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE) for Analysis of Multiprotein Complexes from Cellular Lysates
Published on: February 24, 2011
Myoglobin in a cyanobacterium
M Potts1, S V Angeloni, R E Ebel
1Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg Va 24061.
Summary
A novel myoglobin, cyanoglobin, was discovered in Nostoc commune, a nitrogen-fixing cyanobacterium. This hemoprotein is linked to eukaryotic myoglobins and appears under nitrogen-starved, microaerobic conditions.
Area of Science:
- Biochemistry
- Microbiology
- Molecular Biology
Background:
- Myoglobins are typically found in muscle tissue of animals, functioning in oxygen transport and storage.
- The presence and function of myoglobin-like proteins in prokaryotes, particularly cyanobacteria, remain less understood.
- Nitrogen fixation in cyanobacteria is a complex process sensitive to oxygen levels.
Purpose of the Study:
- To identify and characterize a myoglobin-like protein in the nitrogen-fixing cyanobacterium Nostoc commune.
- To investigate the genetic basis and expression patterns of this novel cyanobacterial hemoprotein.
- To explore the potential role of cyanoglobin in oxygen homeostasis during nitrogen fixation.
Main Methods:
- Isolation and purification of the hemoprotein from Nostoc commune.
- Biochemical characterization including molecular weight determination (12.5 kDa).
- Amino acid sequencing and comparison with known myoglobins.
- Gene identification (glbN) and genomic localization relative to nitrogen fixation genes (nifU, nifH).
- Detection of cyanoglobin expression under specific environmental conditions (nitrogen starvation, microaerobic incubation).
Main Results:
- A soluble hemoprotein, termed cyanoglobin, was identified in Nostoc commune.
- Cyanoglobin exhibits sequence homology to myoglobins from lower eukaryotes like Paramecium and Tetrahymena.
- The cyanoglobin gene (glbN) is located adjacent to essential nitrogen fixation genes.
- Cyanoglobin is specifically detected in cells under nitrogen-starved and microaerobic conditions.
Conclusions:
- Nostoc commune possesses a unique cyanoglobin with evolutionary links to eukaryotic myoglobins.
- The glbN gene's proximity to nif genes suggests a coordinated role in nitrogen fixation.
- Cyanoglobin expression is regulated by nitrogen availability and oxygen levels, potentially aiding in protecting nitrogenase activity.
Related Concept Videos
Antibody Structure
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Protein and Protein Structure
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
A protein's shape is critical to its function. For example, an enzyme can...
Antibody Structure
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Structural Protein Function
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
Fibril-associated Collagen
Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Bacterial Protein Maturation
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

