Related Experiment Video
Updated: Jan 21, 2026
06:40
Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy
Published on: November 4, 2018
6.6K
SecA-Mediated Protein Translocation through the SecYEG Channel
Amalina Ghaisani Komarudin1, Arnold J M Driessen1
1Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, and the Zernike Institute of Advanced Materials, University of Groningen, Nijenborgh 7, 9747AG Groningen, The Netherlands.
Microbiology Spectrum
|August 3, 2019
Summary
The Sec translocase system in bacteria moves proteins across the cell membrane. This system includes the SecYEG channel, SecA motor, and SecDF complex, crucial for bacterial protein transport.
Area of Science:
- Bacterial protein translocation
- Cellular membrane transport mechanisms
- Molecular machinery in prokaryotes
Background:
- The Sec translocase is essential for bacterial viability.
- It facilitates the movement of proteins across the cytoplasmic membrane.
- Key components include SecYEG, SecA, and SecDF.
Purpose of the Study:
- To elucidate the structure and function of the bacterial Sec translocase.
- To provide an overview of the protein translocation machinery.
- To highlight the roles of SecYEG, SecA, and SecDF.
Main Methods:
- Literature review and synthesis of existing research.
- Analysis of structural and functional data on Sec components.
- Discussion of biochemical and genetic studies.
Main Results:
- Detailed description of the SecYEG channel structure.
- Explanation of SecA's role as an ATP-dependent motor.
- Characterization of the SecDF complex's accessory functions.
Conclusions:
- The Sec translocase is a multi-component system vital for bacterial protein export.
- Understanding its structure and function is key to bacterial cell biology.
- Further research can reveal novel targets for antimicrobial strategies.
Related Concept Videos
01:19Translocation of Proteins into the Mitochondria
12.4K
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,...
12.4K
01:20Cotranslational Protein Translocation
9.7K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
9.7K
01:28Protein Translocation Machinery on the ER Membrane
6.6K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
6.6K
01:26Bacterial Translocation and Protein Secretion
558
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
558
01:27Post-translational Translocation of Proteins to the RER
7.6K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
7.6K
01:21G-Protein Gated Ion Channels
5.6K
GPCRs are primarily responsible for our sense of smell, taste, and vision. The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
Sensory...
5.6K