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Full-Text Articles in Life Sciences
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 …
Spatial Sequestration And Oligomer Remodeling During De Novo [Psi+] Formation, Douglas Lyke, Anita L. Manogaran
Spatial Sequestration And Oligomer Remodeling During De Novo [Psi+] Formation, Douglas Lyke, Anita L. Manogaran
Biological Sciences Faculty Research and Publications
Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation. The study of the yeast prion [PSI+], which is the misfolded infectious form of Sup35p, provides a tractable system to monitor prion formation in real time. Recently, we showed that the de novo formation of prion aggregates begins with the appearance of highly mobile cytoplasmic foci, called early foci, which assemble into larger ring or dot structures. We also observed SDS-resistant oligomers during …
Mutations In Mtr4 Structural Domains Reveal Their Important Role In Regulating TrnaI Met Turnover In Saccharomyces Cerevisiae And Mtr4p Enzymatic Activities In Vitro, Yan Li, Joseph Burclaff, James T. Anderson
Mutations In Mtr4 Structural Domains Reveal Their Important Role In Regulating TrnaI Met Turnover In Saccharomyces Cerevisiae And Mtr4p Enzymatic Activities In Vitro, Yan Li, Joseph Burclaff, James T. Anderson
Biological Sciences Faculty Research and Publications
RNA processing and turnover play important roles in the maturation, metabolism and quality control of a large variety of RNAs thereby contributing to gene expression and cellular health. The TRAMP complex, composed of Air2p, Trf4p and Mtr4p, stimulates nuclear exosome-dependent RNA processing and degradation in Saccharomyces cerevisiae. The Mtr4 protein structure is composed of a helicase core and a novel so-called arch domain, which protrudes from the core. The helicase core contains highly conserved helicase domains RecA-1 and 2, and two structural domains of unclear functions, winged helix domain (WH) and ratchet domain. How the structural domains (arch, WH …
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.
Cold Responsive Earli1 Type Hyprps Improve Freezing Survival Of Yeast Cells And Form Higher Order Complexes In Plants, Yi Zhang, Michael Schläppi
Cold Responsive Earli1 Type Hyprps Improve Freezing Survival Of Yeast Cells And Form Higher Order Complexes In Plants, Yi Zhang, Michael Schläppi
Biological Sciences Faculty Research and Publications
Plants have large families of proteins sharing a conserved eight-cysteine-motif (8CM) domain. The biological functions of these proteins are largely unknown. EARLI1 is a cold responsive Arabidopsis gene that encodes a hybrid proline-rich protein (HyPRP) with a three-domain architecture: a putative signal peptide at the N-terminus, a proline-rich domain (PRD) in the middle, and an 8CM domain at the C-terminus. We report here that yeast cells expressing different EARLI1 genes had significantly higher rates of freezing survival than empty-vector transformed controls. Arabidopsis plants with knocked down EARLI1 genes had an increased tendency for freezing-induced cellular damage. EARLI1-GFP Fluorescence in …
Change In Nutritional Status Modulates The Abundance Of Critical Pre-Initiation Intermediate Complexes During Translation Initiation In Vivo, Chingakham Ranjit Singh, Tsuyoshi Udagawa, Bumjun Lee, Sarah Wassink, Hei He, Yasufumi Yamamoto, James T. Anderson, Graham D. Pavitt, Katsura Asano
Change In Nutritional Status Modulates The Abundance Of Critical Pre-Initiation Intermediate Complexes During Translation Initiation In Vivo, Chingakham Ranjit Singh, Tsuyoshi Udagawa, Bumjun Lee, Sarah Wassink, Hei He, Yasufumi Yamamoto, James T. Anderson, Graham D. Pavitt, Katsura Asano
Biological Sciences Faculty Research and Publications
In eukaryotic translation initiation, eIF2∙GTP–Met-tRNAiMet ternary complex (TC) interacts with eIF3–eIF1–eIF5 complex to form the multifactor complex (MFC), while eIF2∙GDP associates with eIF2B for guanine nucleotide exchange. Gcn2p phosphorylates eIF2 to inhibit eIF2B. Here we evaluate the abundance of eIFs and their pre-initiation intermediate complexes in gcn2 deletion mutant grown under different conditions. We show that ribosomes are three times as abundant as eIF1, eIF2 and eIF5, while eIF3 is half as abundant as the latter three and hence, the limiting component in MFC formation. By quantitative immunoprecipitation, we estimate that ∼ 15% of …
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 …