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Related Concept Videos

Proteomics01:33

Proteomics

8.0K
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...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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,...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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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...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
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...
2.6K
Ribosome Profiling02:24

Ribosome Profiling

3.7K
Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
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Preparation of Mitochondrial Enriched Fractions for Metabolic Analysis in Drosophila
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Preparation of Mitochondrial Enriched Fractions for Metabolic Analysis in Drosophila

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Defining mitochondrial protein functions through deep multiomic profiling.

Jarred W Rensvold1,2, Evgenia Shishkova3,4, Yuriy Sverchkov5

  • 1Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO, USA.

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Summary
This summary is machine-generated.

Researchers profiled over 200 mitochondrial protein knockouts to map cellular responses. This study identified new gene functions and a signature for diagnosing mitochondrial disorders.

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Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification
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Area of Science:

  • Cell Biology
  • Genetics
  • Biochemistry

Background:

  • Mitochondria are vital for cellular energy and metabolism.
  • Mitochondrial dysfunction causes over 150 disorders, yet many proteins and genetic causes remain unknown.
  • Understanding mitochondrial protein function is crucial for diagnosing and treating these diseases.

Purpose of the Study:

  • To create a comprehensive functional map of human mitochondrial proteins.
  • To investigate cellular responses to mitochondrial perturbations.
  • To identify novel genes associated with mitochondrial disorders.

Main Methods:

  • Utilized CRISPR-Cas9 gene editing to create over 200 HAP1 cell knockout lines targeting mitochondrial proteins.
  • Performed mass spectrometry-based multiomics analyses to measure cellular responses.
  • Collected approximately 8.3 million biomolecule measurements.

Main Results:

  • Identified PIGY upstream open reading frame (PYURF) as a methyltransferase chaperone involved in complex I assembly and coenzyme Q biosynthesis, linked to a novel mitochondrial disorder.
  • Linked SLC30A9 to mitochondrial ribosomes and oxidative phosphorylation (OxPhos) integrity.
  • Established RAB5IF as a second gene causing cerebrofaciothoracic dysplasia.
  • Generated a comprehensive dataset of mitochondrial protein functions and cellular responses.
  • Discovered a cellular signature indicative of mitochondrial dysfunction.

Conclusions:

  • The study provides a functional compendium of human mitochondrial proteins, aiding in the characterization of orphan proteins.
  • Identified novel gene functions and disease associations, advancing the understanding of mitochondrial disorders.
  • The MITOMICS.app resource facilitates exploration of mitochondrial protein functions and disease mechanisms.
  • The identified cellular signature aids in the genetic diagnosis of mitochondrial diseases.