Related Experiment Video
Updated: Dec 6, 2025

03:09
Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
Published on: August 9, 2024
1.1K
Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase
Marco Túlio Alves da Silva1, Ivan Rosa E Silva1, Lívia Maria Faim1
1Laboratory of Structural Biology, Sao Carlos Institute of Physics, University of São Paulo, São Carlos, SP, Brazil.
Plos Neglected Tropical Diseases
|October 5, 2020
Summary
Selenophosphate synthetase is crucial for parasite survival under endoplasmic reticulum stress. This study reveals its role in regulating stress responses in Trypanosomatidae, impacting parasite viability.
Area of Science:
- Biochemistry
- Molecular Biology
- Parasitology
Background:
- Eukaryotes, particularly Excavata, serve as models for cellular evolution.
- Trypanosomatidae parasites (T. brucei, T. cruzi, L. major) possess complex selenocysteine machinery.
- Selenophosphate synthetase (SEPHS/SPS) is vital for selenocysteine synthesis.
Purpose of the Study:
- To investigate the structural and functional aspects of L. major selenophosphate synthetase.
- To elucidate the role of SEPHS/SPS in Trypanosomatidae cellular processes and stress response.
- To determine the necessity of selenoproteins in parasite viability.
Main Methods:
- Crystal structure determination of L. major SEPHS/SPS.
- Analysis of SEPHS/SPS interactions with other selenocysteine pathway components.
- Gene silencing (RNAi) of SEPHS/SPS and SELENOT in T. brucei under endoplasmic reticulum stress conditions (DTT, tunicamycin).
Main Results:
- The crystal structure of L. major SEPHS/SPS confirmed its functionally important dimeric organization.
- SEPHS/SPS interacts with selenocysteine lyase (SCLY) but not with PSTK-SEPSECS or eEFSec complexes.
- Ablation of SEPHS/SPS in T. brucei caused growth defects under ER stress, suggesting a role in stress response.
- SELENOT was found to be dispensable for parasite viability.
Conclusions:
- T. brucei SEPHS/SPS plays a significant role in regulating the parasite's response to endoplasmic reticulum stress.
- The study highlights the non-essential nature of certain selenoproteins for parasite survival under standard laboratory conditions.
- Structural and functional insights into SEPHS/SPS provide a basis for understanding selenium metabolism in parasites.
More Related Videos
Related Concept Videos
ATP Synthase: Structure
14.5K
ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
14.5K
ATP Synthase: Mechanism
16.2K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.2K
Sulfur Assimilation
220
Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
220
tRNA Activation
21.7K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
21.7K
Enzymes
90.7K
Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
90.7K
Allosteric Proteins-ATCase
6.3K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.3K

