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We began analyzing https://link.springer.com/article/10.1007/s004380051197, but it redirected us to https://link.springer.com/article/10.1007/s004380051197. The analysis below is for the second page.

Title[redir]:
The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1 | Molecular Genetics and Genomics
Description:
Tom1p is a 3268-amino acid protein with extensive homology to the hect-domain class of E3 ubiquitin ligases. Disruption of the TOM1 gene results in temperature sensitivity for growth. Genes encoding the peptidyl proline isomerases Fpr3p and Fpr4p, when present on multicopy plasmids, will suppress this temperature-sensitive growth phenotype. FPR3 can also suppress the mating defect seen in tom1 strains. Suppression is specific for disruption of TOM1, since FPR3 does not restore wild-type growth to strains lacking the E2 ubiquitin-conjugating enzyme Rad6p or the transcriptional regulator Ngg1p. Interestingly, the peptidyl proline isomerase domains of Fpr3p and Fpr4p are not required for suppression; rather the essential sequences include about 170 highly conserved residues at the proteins

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Keywords {πŸ”}

article, fpr, tom, privacy, cookies, content, peptidyl, proline, suppress, information, publish, search, yeast, isomerases, ubiquitin, tomp, protein, fprp, access, data, log, journal, research, molecular, ligase, davey, hannam, wong, gene, growth, strains, suppression, expression, discover, springer, essential, optional, processing, personal, parties, policy, find, track, general, genetics, mgg, high, copy, numbers, defects,

Topics {βœ’οΈ}

3268-amino acid protein proteins' n-termini month download article/chapter restore wild-type growth e3 ubiquitin ligases temperature-sensitive growth phenotype gene regulation privacy choices/manage cookies conditions privacy policy full article pdf related subjects multicopy plasmids european economic area high copy numbers scope submit manuscript hect-domain class transcriptional regulator ngg1p aggregation-prone mutant holistic stability evaluation tom1 gene results tom1 deletion strains essential sequences include accepting optional cookies arg1 promoter found check access instant access suppress defects resulting main content log journal finder publish article molecular tom1p plays article log information privacy policy tom1 strains personal data books a article cite article davey essential cookies optional cookies manage preferences temperature sensitivity suppression molecular features tom1p data protection cookies skip subscription content similar content

Schema {πŸ—ΊοΈ}

WebPage:
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         headline:The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1
         description: Tom1p is a 3268-amino acid protein with extensive homology to the hect-domain class of E3 ubiquitin ligases. Disruption of the TOM1 gene results in temperature sensitivity for growth. Genes encoding the peptidyl proline isomerases Fpr3p and Fpr4p, when present on multicopy plasmids, will suppress this temperature-sensitive growth phenotype. FPR3 can also suppress the mating defect seen in tom1 strains. Suppression is specific for disruption of TOM1, since FPR3 does not restore wild-type growth to strains lacking the E2 ubiquitin-conjugating enzyme Rad6p or the transcriptional regulator Ngg1p. Interestingly, the peptidyl proline isomerase domains of Fpr3p and Fpr4p are not required for suppression; rather the essential sequences include about 170 highly conserved residues at the proteins' N-termini. Previously we found that Tom1p plays a role in gene regulation. Since overexpression of FPR4 does not suppress the reduced expression of the ARG1 promoter found in tom1 deletion strains, Tom1p probably has one or more functions beyond its involvement in gene expression.
         datePublished:
         dateModified:
         pageStart:520
         pageEnd:526
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            Key words Ubiquitin ligase
            Peptidyl proline isomerase
            Yeast
            Multicopy suppression
            Tom1p
            Plant Genetics and Genomics
            Human Genetics
            Microbial Genetics and Genomics
            Animal Genetics and Genomics
            Biochemistry
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                     address:
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                     address:
                        name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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                     address:
                        name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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      headline:The yeast peptidyl proline isomerases FPR3 and FPR4, in high copy numbers, suppress defects resulting from the absence of the E3 ubiquitin ligase TOM1
      description: Tom1p is a 3268-amino acid protein with extensive homology to the hect-domain class of E3 ubiquitin ligases. Disruption of the TOM1 gene results in temperature sensitivity for growth. Genes encoding the peptidyl proline isomerases Fpr3p and Fpr4p, when present on multicopy plasmids, will suppress this temperature-sensitive growth phenotype. FPR3 can also suppress the mating defect seen in tom1 strains. Suppression is specific for disruption of TOM1, since FPR3 does not restore wild-type growth to strains lacking the E2 ubiquitin-conjugating enzyme Rad6p or the transcriptional regulator Ngg1p. Interestingly, the peptidyl proline isomerase domains of Fpr3p and Fpr4p are not required for suppression; rather the essential sequences include about 170 highly conserved residues at the proteins' N-termini. Previously we found that Tom1p plays a role in gene regulation. Since overexpression of FPR4 does not suppress the reduced expression of the ARG1 promoter found in tom1 deletion strains, Tom1p probably has one or more functions beyond its involvement in gene expression.
      datePublished:
      dateModified:
      pageStart:520
      pageEnd:526
      sameAs:https://doi.org/10.1007/s004380051197
      keywords:
         Key words Ubiquitin ligase
         Peptidyl proline isomerase
         Yeast
         Multicopy suppression
         Tom1p
         Plant Genetics and Genomics
         Human Genetics
         Microbial Genetics and Genomics
         Animal Genetics and Genomics
         Biochemistry
         general
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                  address:
                     name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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            name:C. Hannam
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                  address:
                     name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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                  address:
                     name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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         name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
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         name:Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1 E-mail: [email protected]; Tel.: +1-519-661-3908; Fax: +1-519-661-3175, , CA
         type:PostalAddress
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            address:
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            address:
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