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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

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,...
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...
Mitochondrial Protein Sorting01:39

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...
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Protein Transport to the Stroma01:24

Protein Transport to the Stroma

Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...

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mRNA Interactome Capture from Plant Protoplasts
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Processing peptidases in mitochondria and chloroplasts.

Pedro Filipe Teixeira1, Elzbieta Glaser

  • 1Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, SE-106 91 Stockholm, Sweden.

Biochimica Et Biophysica Acta
|April 13, 2012
PubMed
Summary
This summary is machine-generated.

Organelle proteins use targeting peptides for import and are then processed by specific proteases. These proteases ensure correct protein maturation, localization, and organelle function, with some linked to human diseases.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Most mitochondrial and chloroplastic proteins are synthesized in the cytosol with N-terminal targeting peptides.
  • These targeting peptides act as signals for import into organelles, guiding proteins across membranes.
  • After import, targeting peptides are cleaved by specific processing peptidases within the organelles.

Purpose of the Study:

  • To review the roles of organellar proteases in protein processing and quality control.
  • To highlight the peptidases involved in mitochondrial and chloroplast protein maturation.
  • To discuss the implications of protease dysfunction in human diseases.

Main Methods:

  • Review of literature on mitochondrial and chloroplastic protein import and processing.
  • Identification and categorization of key processing peptidases in mitochondria and chloroplasts.
  • Discussion of the functional significance and disease associations of these proteases.

Main Results:

  • Mitochondrial precursor processing involves MPP, MIP (Oct1), Icp55, IMPs, Atp23, rhomboids, and AAA proteases.
  • Chloroplast precursor processing involves SPP, TPP, and CtpA for Photosystem II.
  • Presequence Protease (PreP) degrades cleaved targeting peptides in both organelles.

Conclusions:

  • Organellar proteases form a crucial quality control system for protein maturation and organelle function.
  • Defects in mitochondrial processing proteases are linked to human diseases.
  • Understanding these proteolytic pathways is vital for comprehending organelle homeostasis and disease.