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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Subcellular Fractionation01:32

Subcellular Fractionation

The homogenate obtained after cell lysis contains various membrane-bound organelles that can be further separated into pure fractions by subcellular fractionation. These isolates are used to study specific cellular components, analyze localized protein activity, and are even employed in diagnostics. Fractionation is typically achieved using centrifugation methods, the most common being density-gradient and differential centrifugation.
Differential Centrifugation
Differential centrifugation is...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

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mRNA Interactome Capture from Plant Protoplasts
12:29

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Organelle proteomics.

Sophie Duclos1, Michel Desjardins

  • 1Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, QC, Canada H3T 1J4.

Methods in Molecular Biology (Clifton, N.J.)
|May 24, 2011
PubMed
Summary
This summary is machine-generated.

Proteomics and cell fractionation enhance understanding of cellular functions. Isolating specific cell parts with minimal contamination reveals molecular mechanisms in health and disease.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Proteomics has advanced the understanding of cellular structures and functions over the past decade.
  • Identifying large protein sets from small samples offers insights into cellular mechanisms.

Purpose of the Study:

  • To highlight the importance of proteomics and cell fractionation in studying cellular functions.
  • To emphasize the need for highly enriched cell fractions for accurate organelle analysis.

Main Methods:

  • Utilizing proteomics to identify proteins.
  • Employing various cell fractionation methods for organelle isolation.
  • Analyzing protein content to assess fraction purity.

Main Results:

  • Proteomics enables the identification of numerous proteins from limited biological material.
  • Cell fractionation allows for the isolation of specific cellular organelles.
  • Highly enriched cell fractions are crucial for separating organelles with minimal contamination.

Conclusions:

  • The integration of proteomics and cell fractionation provides unique insights into cellular mechanisms.
  • Successful organelle separation relies on achieving highly pure cellular fractions.
  • This approach is vital for understanding molecular functions in both healthy and diseased states.