The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1

Davey, Michael; Hannam, Carol; Wong, Chun Kwok; Cj, Brandl

doi:10.1007/s004380051197

Cited by 15 publications

(12 citation statements)

References 28 publications

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“…The remaining two distinct nuclear FKBPs are both found in S. cerevisiae (Table 4B). ScFpr3 has been identified as nuclear (Benton et al , 1994; Manning‐Krieg et al , 1994; Shan et al , 1994), as has ScFpr4 (Davey et al , 2000; Dolinski et al , 1997b), with both ScFpr3 and ScFpr4 having been shown to suppress defects seen in the absence of the E3 ubiquitin ligase TOM1 (Davey et al , 2000). SpFKBP39a and CeFkb8 are the only distinct PSORT‐predicted cytoplasmic non‐human FKBPs (Table 4B).…”

Section: Resultsmentioning

confidence: 99%

Identification and comparative analysis of the peptidyl‐prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Pemberton

Kay

2005

Comp Funct Genom

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The peptidyl-prolyl cis/trans isomerase (PPIase) class of proteins comprises three member families that are found throughout nature and are present in all the major compartments of the cell. Their numbers appear to be linked to the number of genes in their respective genomes, although we have found the human repertoire to be smaller than expected due to a reduced cyclophilin repertoire. We show here that whilst the members of the cyclophilin family (which are predominantly found in the nucleus and cytoplasm) and the parvulin family (which are predominantly nuclear) are largely conserved between different repertoires, the FKBPs (which are predominantly found in the cytoplasm and endoplasmic reticulum) are not. It therefore appears that the cyclophilins and parvulins have evolved to perform conserved functions, while the FKBPs have evolved to fill ever-changing niches within the constantly evolving organisms. Many orthologous subgroups within the different PPIase families appear to have evolved from a distinct common ancestor, whereas others, such as the mitochondrial cyclophilins, appear to have evolved independently of one another. We have also identified a novel parvulin within Drosophila melanogaster that is unique to the fruit fly, indicating a recent evolutionary emergence. Interestingly, the fission yeast repertoire, which contains no unique cyclophilins and parvulins, shares no PPIases solely with the budding yeast but it does share a majority with the higher eukaryotes in this study, unlike the budding yeast. It therefore appears that, in comparison with Schizosaccharomyces pombe, Saccharomyces cerevisiae is a poor representation of the higher eukaryotes for the study of PPIases.

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Section: Resultsmentioning

confidence: 99%

Identification and comparative analysis of the peptidyl‐prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Pemberton

Kay

2005

Comp Funct Genom

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“…High-copy FPR3 or FPR4 also suppress ubiquitin ligase tom1 mutations [58]. Tom1 promotes destruction of Dia2, Cdc6 and other proteins [59], [60] and high-copy FPR3 might promote destruction of Tom1 targets similar to Glc7.…”

Section: Discussionmentioning

confidence: 99%

Analysis of Protein Phosphatase-1 and Aurora Protein Kinase Suppressors Reveals New Aspects of Regulatory Protein Function in Saccharomyces cerevisiae

Ghosh

Cannon

2013

PLoS ONE

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Protein phosphatase-1 (PP1) controls many processes in eukaryotic cells. Modulation of mitosis by reversing phosphorylation of proteins phosphorylated by aurora protein kinase is a critical function for PP1. Overexpression of the sole PP1, Glc7, in budding yeast, Saccharomyces cerevisiae, is lethal. This work shows that lethality requires the function of Glc7 regulatory proteins Sds22, Reg2, and phosphorylated Glc8. This finding shows that Glc7 overexpression induced cell death requires a specific subset of the many Glc7-interacting proteins and therefore is likely caused by promiscuous dephosphorylation of a variety of substrates. Additionally, suppression can occur by reducing Glc7 protein levels by high-copy Fpr3 without use of its proline isomerase domain. This divulges a novel function of Fpr3. Most suppressors of GLC7 overexpression also suppress aurora protein kinase, ipl1, temperature-sensitive mutations. However, high-copy mutant SDS22 genes show reciprocal suppression of GLC7 overexpression induced cell death or ipl1 temperature sensitivity. Sds22 binds to many proteins besides Glc7. The N-terminal 25 residues of Sds22 are sufficient to bind, directly or indirectly, to seven proteins studied here including the spindle assembly checkpoint protein, Bub3. These data demonstrate that Sds22 organizes several proteins in addition to Glc7 to perform functions that counteract Ipl1 activity or lead to hyper Glc7 induced cell death. These data also emphasize that Sds22 targets Glc7 to nuclear locations distinct from Ipl1 substrates.

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“…We do not believe that fpr3D acts in mitotic cells to suppress the mitotic DNA-damage checkpoint, because a checkpoint-defective mutation such as rad9D (which is by itself CPT sensitive) does not suppress the CPT sensitivity of rad52-D327. Another possibility is that a prolyl isomerase such as Fpr3 acts in the degradation of mutant proteins (Davey et al 2000). Perhaps Rad52-D327, a truncated protein-or another protein that depends on Rad52 interaction for its stability-is more stable in the absence of Fpr3.…”

Section: Discussionmentioning

confidence: 99%

“…This protein belongs to a very large family of related prolyl isomerases in budding yeast, and their absence has very minor effects on cell viability (Benton et al 1994;Davey et al 2000; http:// db.yeastgenome.org). It is possible that Fpr3 might act to improve the function of Rad51 protein in the absence of its interaction with the C terminus of Rad52.…”

Section: Discussionmentioning

confidence: 99%

Different Mating-Type-Regulated Genes Affect the DNA Repair Defects of Saccharomyces RAD51, RAD52 and RAD55 Mutants

et al. 2006

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Saccharomyces cerevisiae cells expressing both a-and a-mating-type (MAT) genes (termed mating-type heterozygosity) exhibit higher rates of spontaneous recombination and greater radiation resistance than cells expressing only MATa or MATa. MAT heterozygosity suppresses recombination defects of four mutations involved in homologous recombination: complete deletions of RAD55 or RAD57, an ATPase-defective Rad51 mutation (rad51-K191R), and a C-terminal truncation of Rad52, rad52-D327. We investigated the genetic basis of MAT-dependent suppression of these mutants by deleting genes whose expression is controlled by the Mata1-Mata2 repressor and scoring resistance to both campothecin (CPT) and phleomycin. Haploid rad55D strains became more damage resistant after deleting genes required for nonhomologous end-joining (NHEJ), a process that is repressed in MATa/MATa cells. Surprisingly, NHEJ mutations do not suppress CPT sensitivity of rad51-K191R or rad52-D327. However, rad51-K191R is uniquely suppressed by deleting the RME1 gene encoding a repressor of meiosis or its coregulator SIN4; this effect is independent of the meiosis-specific homolog, Dmc1. Sensitivity of rad52-D327 to CPT was unexpectedly increased by the MATa/MATa-repressed gene YGL193C, emphasizing the complex ways in which MAT regulates homologous recombination. The rad52-D327 mutation is suppressed by deleting the prolyl isomerase Fpr3, which is not MATregulated. rad55D is also suppressed by deletion of PST2 and/or YBR052C (RFS1, rad55 suppressor), two members of a three-gene family of flavodoxin-fold proteins that associate in a nonrandom fashion with chromatin. All three recombination-defective mutations are made more sensitive by deletions of Rad6 and of the histone deacetylases Rpd3 and Ume6, although these mutations are not themselves CPT or phleomycin sensitive. D NA repair in budding yeast is strongly influenced by the cell's mating status. Saccharomyces cells can be of three mating types: those able to mate expressing only MATa or only MATa and nonmating cells expressing both MATa and MATa. MATa/MATa diploid cells are more radiation resistant and recombination proficient than diploids expressing only MATa or MATa (Friis and Roman 1968;Heude and Fabre 1993;Fasullo and Dave 1994;Lowell et al. 2003). A similar increase in radioresistance and resistance to radiomimetic drugs is seen in haploid cells that express both mating-type alleles. Coexpression of MATa and MATa, either in diploids or in haploids, leads to the formation of the Mata1-Mata2 corepressor that turns off the expression of haploid-specific genes and induces expression of diploid-specific genes. The most striking effect of a1-a2 repression is a severe disabling of nonhomologous end-joining (NHEJ) by the repression of NEJ1 (Å strö m et al. 1999;Lee et al. 1999; FrankVaillant and Marcand 2001;Kegel et al. 2001;Ooi and Boeke 2001;Valencia et al. 2001). Whether any of the other targets of a1-a2 repression affect homologous recombination (HR) is not known.A double-strand break (DSB) c...

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The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1

Cited by 15 publications

References 28 publications

Identification and comparative analysis of the peptidyl‐prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Identification and comparative analysis of the peptidyl‐prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe

Analysis of Protein Phosphatase-1 and Aurora Protein Kinase Suppressors Reveals New Aspects of Regulatory Protein Function in Saccharomyces cerevisiae

Different Mating-Type-Regulated Genes Affect the DNA Repair Defects of Saccharomyces RAD51, RAD52 and RAD55 Mutants

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