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  • 1
    Language: English
    In: Nature communications, 2014-06-09, Vol.5 (1), p.4091-4091
    Description: DNA double-strand break (DSB) repair is a highly regulated process performed predominantly by non-homologous end joining (NHEJ) or homologous recombination (HR) pathways. How these pathways are coordinated in the context of chromatin is unclear. Here we uncover a role for histone H3K36 modification in regulating DSB repair pathway choice in fission yeast. We find Set2-dependent H3K36 methylation reduces chromatin accessibility, reduces resection and promotes NHEJ, while antagonistic Gcn5-dependent H3K36 acetylation increases chromatin accessibility, increases resection and promotes HR. Accordingly, loss of Set2 increases H3K36Ac, chromatin accessibility and resection, while Gcn5 loss results in the opposite phenotypes following DSB induction. Further, H3K36 modification is cell cycle regulated with Set2-dependent H3K36 methylation peaking in G1 when NHEJ occurs, while Gcn5-dependent H3K36 acetylation peaks in S/G2 when HR prevails. These findings support an H3K36 chromatin switch in regulating DSB repair pathway choice.
    Subject(s): Acetylation ; Acetyltransferases - metabolism ; Chromatin - metabolism ; DNA End-Joining Repair ; DNA Repair ; DNA, Fungal - metabolism ; Histone-Lysine N-Methyltransferase - metabolism ; Histones - metabolism ; Methylation ; Recombinational DNA Repair ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism
    ISSN: 2041-1723
    E-ISSN: 2041-1723
    Source: Nature Open Access
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 2
    Language: English
    In: EMBO reports, 2016-04, Vol.17 (4), p.496-507
    Description: Mis18 is a key regulator responsible for the centromere localization of the CENP‐A chaperone Scm3 in Schizosaccharomyces pombe and HJURP in humans, which establishes CENP‐A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical, and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N‐terminal Yippee‐like domain, is crucial for its centromere localization and function. The crystal structure of the N‐terminal Yippee‐like domain reveals a fold containing a cradle‐shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N‐terminal Yippee‐like domain forms a homodimer in vitro and in vivo, full‐length Mis18, including the C‐terminal α‐helical domain, forms a homotetramer in vitro. We also show that the Yippee‐like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation. Synopsis This study presents the structural characterization of Mis18, a key regulator responsible for the centromere localization of the CENP‐A‐specific chaperone HJURP in humans and Scm3 in S. pombe. While the conserved N‐terminal “Yippee‐like” domain possesses an intrinsic ability to dimerize, the full‐length S. pombe Mis18 forms a tetramer and this oligomeric structure, mediated via its “Yippee‐like” domain, is crucial for Mis18 centromere localization and function. S. pombe Mis18 possesses two structurally distinct domains: an N‐terminal “Yippee‐like” globular domain and a C‐terminal α‐helical domain. While N‐terminal “Yippee‐like” domain possesses an intrinsic ability to homodimerize, the full‐length Mis18 forms a tetramer in vitro. Mutations disrupting the dimerization of “Yippee‐like” domain reduce Mis18 centromere localization and compromise its function. This study presents the structural characterization of Mis18, a key regulator responsible for the centromere localization of the CENP‐A‐specific chaperone HJURP in humans and Scm3 in S. pombe. While the conserved N‐terminal “Yippee‐like” domain possesses an intrinsic ability to dimerize, the full‐length S. pombe Mis18 forms a tetramer and this oligomeric structure, mediated via its “Yippee‐like” domain, is crucial for Mis18 centromere localization and function.
    Subject(s): Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Cycle ; CENP-A ; centromere ; Centromere - genetics ; Centromere - physiology ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Crystal structure ; Crystallography, X-Ray ; DNA Replication, Repair & Recombination ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Epigenesis, Genetic ; epigenetics ; Eukaryotes ; Localization ; Microbiology ; Mis18 ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Protein Domains ; Protein Multimerization ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Scientific Report ; Scientific Reports ; Structural Biology ; Yeast ; Yippee
    ISSN: 1469-221X
    E-ISSN: 1469-3178
    Source: HighWire Press (Free Journals)
    Source: Wiley Online Library All Journals
    Source: PubMed Central
    Source: Get It Now
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  • 3
    Language: English
    In: Open biology, 2012-07, Vol.2 (7)
    Description: The inheritance of the histone H3 variant CENP-A in nucleosomes at centromeres following DNA replication is mediated by an epigenetic mechanism. To understand the process of epigenetic inheritance, or propagation of histones and histone variants, as nucleosomes are disassembled and reassembled in living eukaryotic cells, we have explored the feasibility of exploiting photo-activated localization microscopy (PALM). PALM of single molecules in living cells has the potential to reveal new concepts in cell biology, providing insights into stochastic variation in cellular states. However, thus far, its use has been limited to studies in bacteria or to processes occurring near the surface of eukaryotic cells. With PALM, one literally observes and ‘counts’ individual molecules in cells one-by-one and this allows the recording of images with a resolution higher than that determined by the diffraction of light (the so-called super-resolution microscopy). Here, we investigate the use of different fluorophores and develop procedures to count the centromere-specific histone H3 variant CENP-ACnp1 with single-molecule sensitivity in fission yeast (Schizosaccharomyces pombe). The results obtained are validated by and compared with ChIP-seq analyses. Using this approach, CENP-ACnp1 levels at fission yeast (S. pombe) centromeres were followed as they change during the cell cycle. Our measurements show that CENP-ACnp1 is deposited solely during the G2 phase of the cell cycle.
    Subject(s): 1001 ; 197 ; CENP-A ; centromere ; fission yeast ; Research ; single-molecule microscopy
    E-ISSN: 2046-2441
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
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  • 4
    Language: English
    In: The EMBO journal, 2009-04-08, Vol.28 (7), p.810-820
    Description: To maintain genomic integrity, telomeres must undergo switches from a protected state to an accessible state that allows telomerase recruitment. To better understand how telomere accessibility is regulated in fission yeast, we analysed cell cycle‐dependent recruitment of telomere‐specific proteins (telomerase Trt1, Taz1, Rap1, Pot1 and Stn1), DNA replication proteins (DNA polymerases, MCM, RPA), checkpoint protein Rad26 and DNA repair protein Nbs1 to telomeres. Quantitative chromatin immunoprecipitation studies revealed that MCM, Nbs1 and Stn1 could be recruited to telomeres in the absence of telomere replication in S‐phase. In contrast, Trt1, Pot1, RPA and Rad26 failed to efficiently associate with telomeres unless telomeres are actively replicated. Unexpectedly, the leading strand DNA polymerase ε (Polε) arrived at telomeres earlier than the lagging strand DNA polymerases α (Polα) and δ (Polδ). Recruitment of RPA and Rad26 to telomeres matched arrival of DNA Polε, whereas S‐phase specific recruitment of Trt1, Pot1 and Stn1 matched arrival of DNA Polα. Thus, the conversion of telomere states involves an unanticipated intermediate step where lagging strand synthesis is delayed until telomerase is recruited.
    Subject(s): Cell Cycle ; Cell Cycle Proteins - metabolism ; Chromosomal Proteins, Non-Histone - metabolism ; DNA polymerase ; DNA Polymerase I - metabolism ; DNA Repair ; DNA Replication ; DNA, Fungal - metabolism ; DNA-Directed DNA Polymerase - metabolism ; Genomics ; Molecular biology ; pot1 ; Schizosaccharomyces - enzymology ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism ; telomerase ; Telomerase - metabolism ; Telomere - metabolism ; Yeast
    ISSN: 0261-4189
    E-ISSN: 1460-2075
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
    Source: Get It Now
    Source: Wiley-Blackwell Full Collection 2014
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  • 5
    Language: English
    In: The Journal of biological chemistry, 2019-09-20, Vol.294 (38), p.14119-14134
    Description: The successful assembly and regulation of the kinetochore are critical for the equal and accurate segregation of genetic material during the cell cycle. CENP-C (centromere protein C), a conserved inner kinetochore component, has been broadly characterized as a scaffolding protein and is required for the recruitment of multiple kinetochore proteins to the centromere. At its C terminus, CENP-C harbors a conserved cupin domain that has an established role in protein dimerization. Although the crystal structure of the Saccharomyces cerevisiae Mif2CENP-C cupin domain has been determined, centromeric organization and kinetochore composition vary greatly between S. cerevisiae (point centromere) and other eukaryotes (regional centromere). Therefore, whether the structural and functional role of the cupin domain is conserved throughout evolution requires investigation. Here, we report the crystal structures of the Schizosaccharomyces pombe and Drosophila melanogaster CENP-C cupin domains at 2.52 and 1.81 Å resolutions, respectively. Although the central jelly roll architecture is conserved among the three determined CENP-C cupin domain structures, the cupin domains from organisms with regional centromeres contain additional structural features that aid in dimerization. Moreover, we found that the S. pombe Cnp3CENP-C jelly roll fold harbors an inner binding pocket that is used to recruit the meiosis-specific protein Moa1. In summary, our results unveil the evolutionarily conserved and unique features of the CENP-C cupin domain and uncover the mechanism by which it functions as a recruitment factor.
    Subject(s): analytical ultracentrifugation ; Animals ; BASIC BIOLOGICAL SCIENCES ; Biochemistry & Molecular Biology ; Cell Cycle Proteins - metabolism ; CENP-C ; centromere ; Centromere - metabolism ; Centromere Protein A - metabolism ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomal Proteins, Non-Histone - ultrastructure ; Crystallography, X-Ray - methods ; cupin domain ; Dimerization ; DNA-Binding Proteins - metabolism ; Drosophila melanogaster - metabolism ; Drosophila Proteins - metabolism ; Drosophila Proteins - ultrastructure ; fission yeast ; Histones - metabolism ; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY ; kinetochore ; Kinetochores - metabolism ; Kinetochores - ultrastructure ; Life Sciences & Biomedicine ; meiosis ; Moa1 ; Protein Structure and Folding ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism ; Science & Technology ; X-ray crystallography
    ISSN: 0021-9258
    E-ISSN: 1083-351X
    Source: HighWire Press (Free Journals)
    Source: Web of Science - Science Citation Index Expanded - 2019〈img src="http://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" /〉
    Source: PubMed Central
    Source: Alma/SFX Local Collection
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 6
    Language: English
    In: EMBO reports, 2016-01, Vol.17 (1), p.79-93
    Description: Maintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA‐ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1+ experience both a reduction and mis‐positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re‐establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis‐segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome‐wide. Synopsis Loss of Abo1 function—a bromodomain AAA‐ATPase—results in global perturbations to nucleosome occupancy and organisation with effects on transcription and heterochromatin function. Loss of Abo1 results in a global reduction of histone levels. Nucleosome organisation at gene sequences is perturbed in the absence of Abo1. Abo1 co‐purifies with FACT and suppresses cryptic intragenic transcription. Abo1 function is required for silent centromeric heterochromatin and accurate chromosome segregation. Loss of Abo1 function—a bromodomain AAA‐ATPase—results in global perturbations to nucleosome occupancy and organisation with effects on transcription and heterochromatin function.
    Subject(s): Abo1 ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; bromodomain AAA-ATPases ; Chromatin ; Chromatin - genetics ; Chromatin - metabolism ; Chromatin Assembly and Disassembly ; Chromatin, Epigenetics, Genomics & Functional Genomics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosome Segregation ; DNA, Intergenic ; Gene Silencing ; Genes ; Genomes ; Histone Chaperones - genetics ; Histone Chaperones - metabolism ; Histones - genetics ; Histones - metabolism ; nucleosome mapping ; Nucleosomes - genetics ; Nucleosomes - metabolism ; Promoter Regions, Genetic ; RNA Polymerase II - genetics ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Transcription Factors - metabolism ; Transcription, Genetic
    ISSN: 1469-221X
    E-ISSN: 1469-3178
    Source: HighWire Press (Free Journals)
    Source: Wiley Online Library All Journals
    Source: PubMed Central
    Source: Get It Now
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  • 7
    Language: English
    In: Open biology, 2014-04, Vol.4 (4), p.140043-140043
    Description: CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURPScm3, and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURPScm3 to centromeres is cell cycle regulated. Vertebrate Mis18 associates with Mis18BP1KNL2, which is critical for the recruitment of Mis18 and HJURPScm3. We identify two novel fission yeast Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. Eic1 is essential to maintain Cnp1CENP-A at centromeres and is crucial for kinetochore integrity; Eic2 is dispensable. Eic1 also associates with Fta7CENP-Q/Okp1, Cnl2Nkp2 and Mal2CENP-O/Mcm21, components of the constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1KNL2 orthologue has been identified in fission yeast, consequently it remains unknown how the key Cnp1CENP-A loading factor Mis18 is recruited. Our findings suggest that Eic1 serves a function analogous to that of Mis18BP1KNL2, thus representing the functional counterpart of Mis18BP1KNL2 in fission yeast that connects with a module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated recruitment of the Mis18/Scm3HJURP Cnp1CENP-A loading factors. The novel interactions identified between CENP-A loading factors and the CCAN/Mis6/Ctf19 complex are likely to also contribute to CENP-A maintenance in other organisms.
    Subject(s): 1001 ; 129 ; 197 ; Amino Acid Sequence ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; CENP-A ; Centromere - metabolism ; centromeres ; Chromatin - metabolism ; Chromosomal Proteins, Non-Histone - metabolism ; Cytoskeletal Proteins - chemistry ; Cytoskeletal Proteins - metabolism ; epigenetics ; fission yeast ; Histone Acetyltransferases - metabolism ; Immunoprecipitation ; Kinetochores - chemistry ; Kinetochores - metabolism ; Mis18 ; Molecular Sequence Data ; Mutation ; Protein Binding ; Research ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Sequence Alignment
    ISSN: 2046-2441
    E-ISSN: 2046-2441
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
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  • 8
    Language: English
    In: Molecular and Cellular Biology, 2008-03-01, Vol.28 (5), p.1443-1455
    Description: Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
    Subject(s): Antigens, Nuclear - genetics ; DNA-Binding Proteins - antagonists & inhibitors ; DNA-Binding Proteins - genetics ; Ku Autoantigen ; Plasmids ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Recombination, Genetic ; Schizosaccharomyces - genetics ; Schizosaccharomyces - physiology ; Schizosaccharomyces pombe ; Schizosaccharomyces pombe Proteins - antagonists & inhibitors ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Telomerase - antagonists & inhibitors ; Telomerase - genetics ; Telomere - genetics ; Telomere - physiology ; Telomere-Binding Proteins - antagonists & inhibitors ; Telomere-Binding Proteins - genetics ; Telomere-Binding Proteins - metabolism
    ISSN: 0270-7306
    E-ISSN: 1098-5549
    Source: HighWire Press (Free Journals)
    Source: Hellenic Academic Libraries Link
    Source: PubMed Central
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  • 9
    Language: English
    In: The Journal of biological chemistry, 2010-02-19, Vol.285 (8), p.5327-5337
    Description: When the telomerase catalytic subunit (Trt1/TERT) is deleted, a majority of fission yeast cells survives by circularizing chromosomes. Alternatively, a small minority survives by maintaining telomeric repeats through recombination among telomeres. The recombination-based telomere maintenance in trt1Δ cells is inhibited by the telomere protein Taz1. In addition, catalytically inactive full-length Trt1 (Trt1-CI) and truncated Trt1 lacking the T-motif and reverse transcriptase (RT) domain (Trt1-ΔT/RT) can strongly inhibit recombination-based survival. Here, we investigated the effects of deleting the heterochromatin proteins Swi6 (HP1 ortholog) and Clr4 (Suv39 family of histone methyltransferases) and the telomere capping complex subunits Poz1 and Ccq1 on Taz1- and Trt1-dependent telomere recombination inhibition. The ability of Taz1 to inhibit telomere recombination did not require Swi6, Clr4, Poz1, or Ccq1. Although Swi6, Clr4, and Poz1 were dispensable for the inhibition of telomere recombination by Trt1-CI, Ccq1 was required for efficient telomere recruitment of Trt1 and Trt1-CI-dependent inhibition of telomere recombination. We also found that Swi6, Clr4, Ccq1, the checkpoint kinase Rad3 (ATR ortholog), and the telomerase regulatory subunit Est1 are all required for Trt1-ΔT/RT to inhibit telomere recombination. However, because loss of Swi6, Clr4, Rad3, Ccq1, or Est1 did not significantly alter the recruitment efficiency of Trt1-ΔT/RT to telomeres, these factors are likely to enhance the ability of Trt1-ΔT/RT to inhibit recombination-based survival by contributing to the negative regulation of telomere recombination.
    Subject(s): Aging ; Aging/Telomerase ; Amino Acid Motifs - physiology ; Amino Acid Sequence ; Cancer ; Cell ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell/Checkpoint ; Cell/Cycle ; Checkpoint ; Checkpoint Kinase 2 ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomes, Fungal - genetics ; Chromosomes, Fungal - metabolism ; Cycle ; DNA ; DNA and Chromosomes ; DNA/Protein Interaction ; DNA/Recombination ; DNA/Repair ; DNA/Replication ; Gene Deletion ; Heterochromatin - genetics ; Heterochromatin - metabolism ; Histone-Lysine N-Methyltransferase ; Methyltransferases - genetics ; Methyltransferases - metabolism ; Protein Interaction ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Recombination ; Recombination, Genetic - physiology ; Repair ; Replication ; Schizosaccharomyces - genetics ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Sequence Deletion ; Telomerase ; Telomerase - genetics ; Telomerase - metabolism ; Telomere - genetics ; Telomere - metabolism ; Telomere-Binding Proteins - genetics ; Telomere-Binding Proteins - metabolism
    ISSN: 0021-9258
    E-ISSN: 1083-351X
    Source: HighWire Press (Free Journals)
    Source: PubMed Central
    Source: Alma/SFX Local Collection
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 10
    Language: English
    In: Cell cycle (Georgetown, Tex.), 2010-06-01, Vol.9 (11), p.2237-2248
    Description: While telomeres must provide mechanisms to prevent DNA repair and DNA damage checkpoint factors from fusing chromosome ends and causing permanent cell cycle arrest, these factors associate with functional telomeres and play critical roles in the maintenance of telomeres. Previous studies have established that Tel1 (ATM) and Rad3 (ATR) kinases play redundant but essential roles for telomere maintenance in fission yeast. In addition, the Rad9-Rad1-Hus1 (911) and Rad17-RFC complexes work downstream of Rad3 (ATR) in fission yeast telomere maintenance. Here, we investigated how 911, Rad17-RFC and another RFC-like complex Ctf18-RFC contribute to telomere maintenance in fission yeast cells lacking Tel1 and carrying a novel hypomorphic allele of rad3 (DBD-rad3), generated by the fusion between the DNA binding domain (DBD) of the fission yeast telomere capping protein Pot1 and Rad3. Our investigations have uncovered a surprising redundancy for Rad9 and Hus1 in allowing Rad1 to contribute to telomere maintenance in DBD-rad3 tel1 cells. In addition, we found that Rad17-RFC and Ctf18-RFC carry out redundant telomere maintenance functions in DBD-rad3 tel1 cells. Since checkpoint sensor proteins are highly conserved, genetic redundancies uncovered here may be relevant to telomere maintenance and detection of DNA damage in other eukaryotes.
    Subject(s): Alleles ; Binding ; Biology ; Bioscience ; Calcium ; Cancer ; Carrier Proteins - metabolism ; Carrier Proteins - physiology ; Cell ; Cell Cycle Proteins - metabolism ; Cell Cycle Proteins - physiology ; checkpoint ; Checkpoint Kinase 2 ; Ctf18 ; Cycle ; DNA - chemistry ; DNA-Binding Proteins - metabolism ; DNA-Binding Proteins - physiology ; Endonucleases - metabolism ; Endonucleases - physiology ; Landes ; Organogenesis ; Protein Kinases - metabolism ; Protein Kinases - physiology ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Serine-Threonine Kinases - physiology ; Proteins ; Rad17 ; Rad9-Rad1-Hus1 ; Schizosaccharomyces - metabolism ; Schizosaccharomyces pombe Proteins - metabolism ; Schizosaccharomyces pombe Proteins - physiology ; telomere ; Telomere - metabolism ; Transcription Factors - metabolism ; Transcription Factors - physiology
    ISSN: 1538-4101
    E-ISSN: 1551-4005
    Source: PubMed Central
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