scholarly journals MDP1, a Saccharomyces cerevisiae Gene Involved in Mitochondrial/Cytoplasmic Protein Distribution, Is Identical to the Ubiquitin-Protein Ligase Gene RSP5

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 595-603 ◽  
Author(s):  
Teresa Żołądek ◽  
Anna Tobiasz ◽  
Gabriela Vaduva ◽  
Magda Boguta ◽  
Nancy C Martin ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Subcellular Distribution ◽  
Nonsense Suppression ◽  
Protein Distribution ◽  
Multicopy Suppressor ◽  
Ubiquitin Protein Ligase ◽  
Cytoskeleton Organization ◽  
Isolation And Characterization ◽  
Initiation Of Translation

Alteration of the subcellular distribution of Mod5p-I, a tRNA modification enzyme, member of the sorting isozyme family, affects tRNA-mediated nonsense suppression. Altered suppression efficiency was used to identify MDP genes, which, when mutant, change the mitochondrial/cytosolic distribution of Mod5p-I,KR6. MDP2 is the previously identified VRP1, which encodes verprolin, required for proper organization of the actin cytoskeleton. MDP3 is identical to PAN1, which encodes a protein involved in initiation of translation and actin cytoskeleton organization. We report here the cloning and characterization of wild-type and mutant MDP1 alleles and the isolation and characterization of a multicopy suppressor of mdp1 mutations. MDP1 is identical to RSP5, which encodes ubiquitin-protein ligase, and mdp1 mutations are suppressed by high copy expression of ubiquitin. All four characterized mdp1 mutations cause missense changes located in the hect domain of Rsp5p that is highly conserved among ubiquitin-protein ligases. In addition to its well-known function in protein turnover, ubiquitination has been proposed to play roles in subcellular sorting of proteins via endocytosis and in delivery of proteins to peroxisomes, the endoplasmic reticulum and mitochondria. mdp1, as well as mdp2/vrp1 and mdp3/pan1 mutations, affect endocytosis. Further, mdp1 mutations show synthetic interactions with mdp2/vrp1 and mdp3/pan1. Identification of MDP1 as RSP5, along with our previous identification of MDP2/VRP1 and MDP3/PAN1, implicate interactions of the ubiquitin system, the actin cytoskeleton and protein synthesis in the subcellular distribution of proteins.

scholarly journals Characterization of Staphylococcus intermedius Group Isolates Associated with Animals from Antarctica and Emended Description of Staphylococcus delphini

2020 ◽  
Vol 8 (2) ◽  
pp. 204 ◽  
Author(s):  
Veronika Vrbovská ◽  
Ivo Sedláček ◽  
Michal Zeman ◽  
Pavel Švec ◽  
Vojtěch Kovařovic ◽  
...  
Keyword(s):  
Rpob Gene ◽  
Protein Distribution ◽  
Pathogenic Potential ◽  
Weddell Seals ◽  
Polymerase Beta ◽  
Flight Mass Spectrometry ◽  
Isolation And Characterization ◽  
Staphylococcus Intermedius ◽  
The Antarctic

Members of the genus Staphylococcus are widespread in nature and occupy a variety of niches, however, staphylococcal colonization of animals in the Antarctic environment has not been adequately studied. Here, we describe the first isolation and characterization of two Staphylococcus intermedius group (SIG) members, Staphylococcus delphini and Staphylococcus pseudintermedius, in Antarctic wildlife. Staphylococcus delphini were found exclusively in Adélie penguins. The report of S. pseudintermedius from Weddell seals confirmed its occurrence in all families of the suborder Caniformia. Partial RNA polymerase beta-subunit (rpoB) gene sequencing, repetitive PCR fingerprinting with the (GTG)5 primer, and matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry gave consistent identification results and proved to be suitable for identifying SIG members. Comparative genomics of S. delphini isolates revealed variable genomic elements, including new prophages, a novel phage-inducible chromosomal island, and numerous putative virulence factors. Surface and extracellular protein distribution were compared between genomes and showed strain-specific profiles. The pathogenic potential of S. delphini was enhanced by a novel type of exfoliative toxin, trypsin-like serine protease cluster, and enterotoxin C. Detailed analysis of phenotypic characteristics performed on six Antarctic isolates of S. delphini and eight reference strains from different animal sources enabled us to emend the species description of S. delphini.

scholarly journals Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis in mitochondrial delivery.

1995 ◽  
Vol 15 (12) ◽  
pp. 6884-6894 ◽  
Author(s):  
T Zoladek ◽  
G Vaduva ◽  
L A Hunter ◽  
M Boguta ◽  
B D Go ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Actin Cytoskeleton ◽  
Selection Strategy ◽  
Cell Fractionation ◽  
Gene Products ◽  
Protein Distribution ◽  
Cytoskeleton Organization ◽  
Molecular Approaches ◽  
Apply Genetic ◽  
Cell Biol

The Saccharomyces cerevisiae MOD5 gene encodes proteins that function in three subcellular locations: mitochondria, the cytoplasm, and nuclei (M. Boguta, L.A. Hunter, W.-C. Shen, E. C. Gillman, N. C. Martin, and A. K. Hopper, Mol. Cell. Biol. 14:2298-2306, 1994; E. C. Gillman, L. B. Slusher, N. C. Martin, and A. K. Hopper, Mol. Cell. Biol. 11:2382-2390, 1991). A mutant allele of MOD5 encoding a protein (Mod5p-I,KR6) located predominantly in mitochondria was constructed. Mutants defective in delivering Mod5p-I,KR6 to mitochondria were sought by selecting cells with increased cytosolic activity of this protein. Twenty-five mutants defining four complementation groups, mdp1, mdp2, mdp3, and mdp4, were found. They are unable to respire at 34 degrees C or to grow on glucose medium at 38 degrees C. Cell fractionation studies showed that mdp1, mdp2, and mdp3 mutants have an altered mitochondrial-cytoplasmic distribution of Mod5p. mdp2 can be suppressed by ACT1, the actin-encoding gene. The actin cytoskeleton organization is also aberrant in mdp2 cells. MDP2 is the same as VRP1 (S. F. H. Donnelly, M. J. Picklington, D. Pallotta, and E. Orr, Mol. Microbiol. 10:585-596, 1993). MDP3 is identical to PAN1, which encodes a protein that interacts with mRNA 3' ends and affects initiation of protein synthesis (A. B. Sachs and J. A. Deardoff, Cell 70:961-973, 1992). These results implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis as being as important for protein distribution in S. cerevisiae as they are for distribution of cytosolic proteins in higher eukaryotes. This provides the potential to apply genetic and molecular approaches to study gene products and mechanisms involved in this type of protein distribution. The selection strategy also offers a new approach for identifying gene products involved in the distribution of proteins to their subscellular destinations.

scholarly journals Isolation and Characterization of the Saccharomyces cerevisiae XPT1 Gene Encoding Xanthine Phosphoribosyl Transferase

1999 ◽  
Vol 181 (9) ◽  
pp. 2984-2986 ◽  
Author(s):  
M. L. Guetsova ◽  
T. R. Crother ◽  
M. W. Taylor ◽  
B. Daignan-Fornier
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Hypoxanthine Phosphoribosyl Transferase ◽  
Gene Encoding ◽  
Multicopy Suppressor ◽  
Phosphoribosyl Transferase ◽  
Isolation And Characterization ◽  
Severe Reduction

ABSTRACT A new Saccharomyces cerevisiae gene, XPT1, was isolated as a multicopy suppressor of a hypoxanthine phosphoribosyl transferase (HPRT) defect. Disruption of XPT1 affects xanthine utilization in vivo and results in a severe reduction of xanthine phosphoribosyl transferase (XPRT) activity while HPRT is unaffected. We conclude that XPT1 encodes XPRT in yeast.

The isolation and characterization of 18 equine microsatellite loci, TKY272–TKY289

2000 ◽  
Vol 31 (2) ◽  
pp. 149-149 ◽  
Author(s):  
T Tozaki ◽  
H Kakoi ◽  
S Mashima ◽  
K Hirota ◽  
T Hasegawa ◽  
...  
Keyword(s):  
Microsatellite Loci ◽  
Isolation And Characterization
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