Related Experiment Video
Updated: May 15, 2026
05:34
Sexual Crosses with the Mucoromycete Phycomyces blakesleeanus
Published on: June 6, 2025
Correlation between sequence, structure and function for trisporoid processing proteins in the model zygomycete Mucor
Sabrina Ellenberger1, Stefan Schuster, Johannes Wöstemeyer
1Institute of General Microbiology and Microbial Genetics, Friedrich Schiller University Jena, 07743 Jena, Neugasse 24, Germany. Sabrina.Ellenberger@uni-jena.de
Journal of Theoretical Biology
|December 25, 2012
Summary
Trisporoids act as fungal pheromones, crucial for mating in ancient fungi. Researchers studied trisporic acid synthesis proteins (TSP1 and TSP2), revealing conserved active sites despite different structures, aiding in understanding evolutionary relationships.
Area of Science:
- Biochemistry
- Mycology
- Structural Biology
Background:
- Terpenoids, including trisporoids, play vital roles in biological systems.
- Trisporoids function as essential pheromones in mucoralean zygomycetes, mediating mating partner recognition and sexual reproduction.
- Trisporoids are synthesized via β-carotene degradation and share structural similarities with retinoids and abscisic acid.
Purpose of the Study:
- To investigate evolutionary relationships among proteins involved in trisporoid binding.
- To identify functionally related proteins through sequence and structure comparisons.
- To elucidate the structural basis of trisporoid synthesis and binding.
Main Methods:
- Calculation of three-dimensional structures for 4-dihydromethyltrisporate dehydrogenase (TSP1) and 4-dihydrotrisporin dehydrogenase (TSP2).
- Protein structure comparison focusing on conserved functional domains.
- Molecular docking studies to determine ligand binding sites for NADP and trisporoid ligands.
Main Results:
- TSP1, an aldo-keto reductase, exhibits a TIM-barrel structure, while TSP2, a short-chain dehydrogenase, has a Rossmann fold.
- Functional conservation of enzymes can be independent of their core protein structure.
- Docking studies revealed comparable active site surfaces between TSP1 and TSP2, with distinct trisporoid binding preferences (open vs. closed regions).
Conclusions:
- Despite significant differences in amino acid sequence and tertiary structure, TSP1 and TSP2 share comparable active site surfaces, indicating functional convergence.
- The identified binding regions and docking models provide insights into substrate specificity and the mechanism of trisporoid recognition.
- This study enhances understanding of the evolution of enzymes involved in fungal pheromone synthesis.
Related Concept Videos
01:29Fungal Group Zygomycota
Zygomycota, previously classified as a distinct fungal group, are primarily terrestrial, saprophytic molds that play a crucial role as decomposers. Recent phylogenetic studies have revealed that these fungi are now divided into two major clades — Mucoromycota, which includes many symbiotic species, and Zoopagomycota, which primarily consists of parasitic and pathogenic fungi. These groups exhibit distinct ecological roles and reproductive strategies while sharing key structural and...
01:56Structural 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...
01:56Structural 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...
01:21Structure of Porins
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
02:41Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
01:19Septins
Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...