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Full-Text Articles in Life Sciences
Hypoxia-Inducible Gene Domain 1 Proteins In Yeast Mitochondria Protect Against Proton Leak Through Complex Iv, Ngoc H. Hoang, Vera Strogolova, Jaramys J. Mosley, Rosemary A. Stuart, Jonathan Hosler
Hypoxia-Inducible Gene Domain 1 Proteins In Yeast Mitochondria Protect Against Proton Leak Through Complex Iv, Ngoc H. Hoang, Vera Strogolova, Jaramys J. Mosley, Rosemary A. Stuart, Jonathan Hosler
Biological Sciences Faculty Research and Publications
Hypoxia-inducible gene domain 1 (HIGD1) proteins are small integral membrane proteins, conserved from bacteria to humans, that associate with oxidative phosphorylation supercomplexes. Using yeast as a model organism, we have shown previously that its two HIGD1 proteins, Rcf1 and Rcf2, are required for the generation and maintenance of a normal membrane potential (ΔΨ) across the inner mitochondrial membrane (IMM). We postulated that the lower ΔΨ observed in the absence of the HIGD1 proteins may be due to decreased proton pumping by complex IV (CIV) or enhanced leak of protons across the IMM. Here we measured the ΔΨ generated by complex …
The Yeast Mitochondrial Proteins Rcf1 And Rcf2 Support The Enzymology Of The Cytochrome C Oxidase Complex And Generation Of The Proton Motive Force, Vera Strogolova, Ngoc H. Hoang, Jonathan Hosler, Rosemary A. Stuart
The Yeast Mitochondrial Proteins Rcf1 And Rcf2 Support The Enzymology Of The Cytochrome C Oxidase Complex And Generation Of The Proton Motive Force, Vera Strogolova, Ngoc H. Hoang, Jonathan Hosler, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
The yeast mitochondrial proteins Rcf1 and Rcf2 are associated with a subpopulation of the cytochrome bc1–cytochrome c oxidase supercomplex and have been proposed to play a role in the assembly and/or modulation of the activity of the cytochrome c oxidase (complex IV, CIV). Yeast mutants deficient in either Rcf1 or Rcf2 proteins can use aerobic respiration–based metabolism for growth, but the absence of both proteins results in a strong growth defect. In this study, using assorted biochemical and biophysical analyses of Rcf1/Rcf2 single and double null-mutant yeast cells and mitochondria, we further explored how Rcf1 and Rcf2 support …
Mutational Analysis Of The Qrrq Motif In The Yeast Hig1 Type 2 Protein Rcf1 Reveals A Regulatory Role For The Cytochrome C Oxidase Complex, Joshua Garlich, Valentina Strecker, Ilka Wittig, Rosemary A. Stuart
Mutational Analysis Of The Qrrq Motif In The Yeast Hig1 Type 2 Protein Rcf1 Reveals A Regulatory Role For The Cytochrome C Oxidase Complex, Joshua Garlich, Valentina Strecker, Ilka Wittig, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
The yeast Rcf1 protein is a member of the conserved family of proteins termed the hypoxia-induced gene (domain) 1 (Hig1 or HIGD1) family. Rcf1 interacts with components of the mitochondrial oxidative phosphorylation system, in particular the cytochrome bc1(complex III)-cytochrome c oxidase (complex IV) supercomplex (termed III-IV) and the ADP/ATP carrier proteins. Rcf1 plays a role in the assembly and modulation of the activity of complex IV; however, the molecular basis for how Rcf1 influences the activity of complex IV is currently unknown. Hig1 type 2 isoforms, which include the Rcf1 protein, are characterized in part by the presence …
Truncation Of The Mrp20 Protein Reveals New Ribosome‐Assembly Subcomplex In Mitochondria, Jasvinder Kaur, Rosemary A. Stuart
Truncation Of The Mrp20 Protein Reveals New Ribosome‐Assembly Subcomplex In Mitochondria, Jasvinder Kaur, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
Mitochondrial ribosomal protein 20 (Mrp20) is a component of the yeast mitochondrial large (54S) ribosomal subunit and is homologous to the bacterial L23 protein, located at the ribosomal tunnel exit site. The carboxy‐terminal mitochondrial‐specific domain of Mrp20 was found to have a crucial role in the assembly of the ribosomes. A new, membrane‐bound, ribosomal‐assembly subcomplex composed of known tunnel‐exit‐site proteins, an uncharacterized ribosomal protein, MrpL25, and the mitochondrial peroxiredoxin (Prx), Prx1, accumulates in an mrp20ΔC yeast mutant. Finally, data supporting the idea that the inner mitochondrial membrane acts as a platform for the ribosome assembly process are discussed.
Mitochondrial Biogenesis: Is An Old Dog Still Teaching Us New Tricks? Meeting On The Assembly Of The Mitochondrial Respiratory Chain, Rosemary A. Stuart, Peter Rehling
Mitochondrial Biogenesis: Is An Old Dog Still Teaching Us New Tricks? Meeting On The Assembly Of The Mitochondrial Respiratory Chain, Rosemary A. Stuart, Peter Rehling
Biological Sciences Faculty Research and Publications
No abstract provided.
Yeast Oxa1 Interacts With Mitochondrial Ribosomes: The Importance Of The C‐Terminal Region Of Oxa1, Lixia Jia, Mary Kathryn Dienhart, Mark Schramp, Matthew Mccauley, Kai Hell, Rosemary A. Stuart
Yeast Oxa1 Interacts With Mitochondrial Ribosomes: The Importance Of The C‐Terminal Region Of Oxa1, Lixia Jia, Mary Kathryn Dienhart, Mark Schramp, Matthew Mccauley, Kai Hell, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
The yeast mitochondrial Oxa1 protein is a member of the conserved Oxa1/YidC/Alb3 protein family involved in the membrane insertion of proteins. Oxa1 mediates the insertion of proteins (nuclearly and mitochondrially encoded) into the inner membrane. The mitochondrially encoded substrates interact directly with Oxa1 during their synthesis as nascent chains and in a manner that is supported by the associated ribosome. We have investigated if the Oxa1 complex interacts with the mitochondrial ribosome. Evidence to support a physical association between Oxa1 and the large ribosomal subunit is presented. Our data indicate that the matrix‐exposed C‐terminal region of Oxa1 plays an important …
Insertion Of Proteins Into The Inner Membrane Of Mitochondria: The Role Of The Oxa1 Complex, Rosemary A. Stuart
Insertion Of Proteins Into The Inner Membrane Of Mitochondria: The Role Of The Oxa1 Complex, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
The inner mitochondrial membrane harbors a large number of proteins that display a wide range of topological arrangements. The majority of these proteins are encoded in the cell's nucleus, but a few polytopic proteins, all subunits of respiratory chain complexes are encoded by the mitochondrial genome. A number of distinct sorting mechanisms exist to direct these proteins into the mitochondrial inner membrane. One of these pathways involves the export of proteins from the matrix into the inner membrane and is used by both proteins synthesized within the mitochondria, as well as by a subset of nuclear encoded proteins. Prior to …
Oxa1p Acts As A General Membrane Insertion Machinery For Proteins Encoded By Mitochondrial Dna, Kai Hell, Walter Neupert, Rosemary A. Stuart
Oxa1p Acts As A General Membrane Insertion Machinery For Proteins Encoded By Mitochondrial Dna, Kai Hell, Walter Neupert, Rosemary A. Stuart
Biological Sciences Faculty Research and Publications
Oxa1p is a member of the conserved Oxa1/YidC/Alb3 protein family involved in the membrane insertion of proteins. Oxa1p has been shown previously to directly facilitate the export of the N‐terminal domains of membrane proteins across the inner membrane to the intermembrane space of mitochondria. Here we report on a general role of Oxa1p in the membrane insertion of proteins. (i) The function of Oxa1p is not limited to the insertion of membrane proteins that undergo N‐terminal tail export; rather, it also extends to the insertion of other polytopic proteins such as the mitochondrially encoded Cox1p and Cox3p proteins. These are …