Related Experiment Video
Updated: May 5, 2026
09:54
Isolation and Respiratory Measurements of Mitochondria from Arabidopsis thaliana
Published on: January 5, 2018
14.6K
Carnitine short-chain acyltransferase in pea mitochondria
C Wood1, M Noh Hj Jalil, A Ariffin
1Department of Plant Biology, The University, NE1 7RU, Newcastle upon Tyne, UK.
Planta
|November 23, 2013
Summary
Carnitine acetyltransferase is present in pea mitochondria. Acetyl-carnitine can be exported from mitochondria to the cytoplasm efficiently.
Area of Science:
- Biochemistry
- Plant Physiology
- Mitochondrial Function
Background:
- Carnitine acetyltransferase (CAT) plays a crucial role in cellular energy metabolism by interconverting acetyl-CoA and carnitine.
- Understanding the localization and function of CAT in plant mitochondria is essential for elucidating energy transport mechanisms.
Purpose of the Study:
- To investigate the presence and potential function of carnitine acetyltransferase in pea (Pisum sativum) cotyledon mitochondria.
- To explore the feasibility of acetyl-carnitine export from the mitochondrial matrix to the extra-mitochondrial space.
Main Methods:
- Mitochondrial isolation from pea cotyledons.
- Enzyme assays to detect carnitine acetyltransferase activity.
- Subcellular localization studies.
Main Results:
- Carnitine acetyltransferase activity was confirmed in pea cotyledon mitochondria.
- Evidence suggests that acetyl-carnitine can be exported from the mitochondrial matrix to extra-mitochondrial sites.
- The export process appears to occur without significant energy loss.
Conclusions:
- Pea cotyledon mitochondria possess carnitine acetyltransferase activity.
- Acetyl-carnitine can be efficiently transported out of the mitochondria, suggesting a role in inter-organelle metabolic communication.
More Related Videos
08:55Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
Published on: July 19, 2021
2.6K
14:42Liquid Chromatography Coupled to Refractive Index or Mass Spectrometric Detection for Metabolite Profiling in Lysate-based Cell-free Systems
Published on: September 23, 2021
6.7K
Related Concept Videos
01:19Translocation of Proteins into the Mitochondria
8.8K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.8K
01:48ATP Synthase: Mechanism
16.0K
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...
16.0K
01:37Energy to Drive Translocation
2.0K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.0K
01:39Mitochondrial Protein Sorting
4.4K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.4K
01:42The ADP/ATP Carrier Protein
3.6K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
3.6K
01:18Protein Transport to the Inner Chloroplast Membrane
1.7K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
1.7K