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Related Concept Videos

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...
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 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 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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Related Experiment Video

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Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae
08:55

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Published on: July 19, 2021

Her2p molecular modeling, mutant analysis and intramitochondrial localization.

José Ribamar Ferreira-Júnior1, Lucas Bleicher, Mario H Barros

  • 1Escola de Artes, Ciências e Humanidades - USP, Brazil.

Fungal Genetics and Biology : FG & B
|July 16, 2013
PubMed
Summary

Mitochondrial GatFAB amidotransferase complex, crucial for protein synthesis, involves Her2p. This study reveals Her2p

Keywords:
AmidotransferaseGatFABMitochondria translationPAGEPCRPMSFPhenylmethanesulfonyl fluorideSDSglutamyl-tRNAGlnmitochondrial DNAmtDNApolyacrylamide gel electrophoresispolymerase chain reactionrespiratory deficient mutant lacking mitochondrial DNArespiratory deficient mutant with a partially deleted mitochondrial genomesodium dodecyl sulfatetemperature sensitive mutanttsρ(o) mutantρ(−) mutant

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Area of Science:

  • Mitochondrial protein synthesis and quality control.
  • Enzyme complex structure and function.
  • Molecular biology and genetics.

Background:

  • Bacterial GatCAB amidotransferases catalyze tRNA transamidation.
  • Mitochondria possess a GatFAB amidotransferase complex for glutamyl-tRNA(Gln) transamidation.
  • Her2p, Gtf1p, and Pet112p are key components of the mitochondrial GatFAB complex.

Purpose of the Study:

  • To investigate the HER2 protein family using molecular modeling and amino acid correlation analysis.
  • To elucidate the localization and function of Her2p within the mitochondrial environment.
  • To identify key residues in Her2p contributing to complex stability and function.

Main Methods:

  • Molecular modeling and amino acid correlation analysis of the HER2 protein family.
  • Subcellular localization studies using microscopy.
  • Random mutagenesis of HER2 and analysis of mutant phenotypes.
  • Genetic analysis involving gene overexpression (GTF1, PET112).

Main Results:

  • Her2p localizes to both the mitochondrial outer membrane and matrix.
  • Her2p, Pet112p, and Gtf1p form the mitochondrial GatFAB complex.
  • Mutagenesis identified residues critical for complex thermostability.
  • Specific mutations in HER2 impaired fermentative growth and were poorly rescued by GTF1 overexpression.
  • Her2p's outer membrane function impacts cell viability.

Conclusions:

  • Her2p plays a dual role in mitochondria, participating in the GatFAB complex and having an uncharacterized function in the outer membrane.
  • The stability and function of the GatFAB complex are sensitive to specific HER2 residues and genetic interactions.
  • Her2p's mitochondrial outer membrane role is essential for cell viability, particularly under specific growth conditions.