Related Experiment Video
Updated: Aug 4, 2026

09:33
Rapid Isolation of the Mitoribosome from HEK Cells
Published on: October 4, 2018
Mitochondrial protein synthesis may be involved in long-term memory formation
1Department of Physiology, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Pharmacology, Biochemistry, and Behavior
|April 1, 1989
Summary
Two stages of protein synthesis are essential for forming long-term memory (LTM) in rats. Cytoplasmic protein synthesis is needed early, while mitochondrial protein synthesis occurs later, both crucial for memory consolidation.
Area of Science:
- Neuroscience
- Molecular Biology
- Behavioral Neuroscience
Background:
- Long-term memory (LTM) formation is a complex process.
- Protein synthesis (PS) is known to play a role in memory consolidation.
- The specific temporal and spatial requirements of PS in LTM remain under investigation.
Purpose of the Study:
- To investigate the hypothesis that two distinct stages of cerebral protein synthesis are required for LTM formation in rats.
- To differentiate the roles of cytoplasmic and mitochondrial protein synthesis in memory consolidation.
Main Methods:
- Rats were trained on an active-avoidance task.
- Cytoplasmic protein synthesis was inhibited using anisomycin (ANI).
- Mitochondrial protein synthesis was inhibited using chloramphenicol (CAP).
- Inhibitors were administered at various time points before and after training.
Main Results:
- Inhibition of cytoplasmic PS with ANI before training prevented LTM formation.
- Anisomycin administered after training was ineffective in preventing LTM.
- Chloramphenicol inhibition of mitochondrial PS between 15 and 55 minutes post-training interfered with LTM formation.
- Mitochondrial PS inhibition prior to 15 minutes or after 55 minutes post-training did not affect LTM.
Conclusions:
- Two distinct, sequential stages of protein synthesis are necessary for LTM formation.
- The first stage involves cytoplasmic PS, initiated at the start of training and independent of new mRNA.
- The second stage involves mitochondrial PS, beginning around 25 minutes post-training and dependent on newly synthesized mRNA.
Related Concept Videos
Ribosomal RNA Synthesis
Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
ATP Synthase: Mechanism
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 ATP...
Mitochondrial Protein Sorting
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...
Mitochondrial Precursor Proteins
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Most of the mitochondrial precursors...
Translocation of Proteins into the Mitochondria
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,...
Porin Insertion in the Outer Mitochondrial Membrane
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

