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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Mitochondrial Precursor Proteins01:39

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 25, 2026

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
08:23

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data

Published on: February 18, 2022

ORC proteins: marking the start.

Dale B Wigley1

  • 1Cancer Research UK Clare Hall Laboratories, The London Research Institute, Blanche Lane, South Mimms, Potters Bar, Herts, UK. Dale.Wigley@cancer.org.uk

Current Opinion in Structural Biology
|February 17, 2009
PubMed
Summary
This summary is machine-generated.

Archaea possess DNA replication machinery similar to eukaryotes, featuring multiple replication origins. While protein-DNA interactions at these origins are becoming clearer, the precise mechanisms of origin assembly and firing remain unknown.

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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

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Last Updated: Jun 25, 2026

De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
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Published on: February 18, 2022

Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The DNA replication machinery in archaea shares more similarities with eukaryotes than with eubacteria.
  • Archaea, similar to eukaryotes, utilize multiple replication origins for DNA duplication.
  • Understanding archaeal DNA replication is crucial for insights into eukaryotic replication mechanisms.

Purpose of the Study:

  • To elucidate the molecular mechanisms of DNA replication origin recognition and remodeling in archaea.
  • To investigate the structural basis of archaeal origin binding proteins interacting with DNA.
  • To identify the remaining gaps in knowledge regarding archaeal origin assembly and firing.

Main Methods:

  • Analysis of biochemical data on archaeal origin binding proteins.
  • Determination of crystal structures of archaeal replication origin binding proteins bound to DNA.
  • Comparative analysis of archaeal and eukaryotic DNA replication systems.

Main Results:

  • Archaea exhibit DNA replication apparatus closely related to eukaryotes.
  • Crystal structures reveal how archaeal origin binding proteins deform DNA upon binding.
  • Detailed insights into the initial protein-DNA interactions at archaeal replication origins were obtained.

Conclusions:

  • Archaea provide a valuable model for studying eukaryotic DNA replication.
  • Significant progress has been made in understanding protein-DNA interactions at archaeal replication origins.
  • The molecular mechanisms governing the assembly and firing of archaeal replication origins still require further investigation.