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Article ; Online: Mis16 Switches Function from a Histone H4 Chaperone to a CENP-A

An, Sojin / Koldewey, Philipp / Chik, Jennifer / Subramanian, Lakxmi / Cho, Uhn-Soo

Structure (London, England : 1993)

2018 Volume 26, Issue 7, Page(s) 960–971.e4

Abstract: The Mis18 complex, composed of Mis16, Eic1, and Mis18 in fission yeast, selectively deposits the centromere-specific histone H3 variant, CENP- ... ...

Abstract	The Mis18 complex, composed of Mis16, Eic1, and Mis18 in fission yeast, selectively deposits the centromere-specific histone H3 variant, CENP-A
MeSH term(s)	Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Crystallography, X-Ray ; Histones/metabolism ; Models, Molecular ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Protein Multimerization ; Schizosaccharomyces/chemistry ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Carrier Proteins ; Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; Histones ; Mis16 protein, S pombe ; Mis18 protein, S pombe ; Mis19 protein, S pombe ; Multiprotein Complexes ; Schizosaccharomyces pombe Proteins
Language	English
Publishing date	2018-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2018.04.012
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Article ; Online: To fuse or not to fuse: how do checkpoint and DNA repair proteins maintain telomeres?

Subramanian, Lakxmi / Nakamura, Toru M

Frontiers in bioscience (Landmark edition)

2010 Volume 15, Issue 3, Page(s) 1105–1118

Abstract: DNA damage checkpoint and DNA repair mechanisms play critical roles in the stable maintenance of genetic information. Various forms of DNA damage that arise inside cells due to common errors in normal cellular processes, such as DNA replication, or due ... ...

Abstract	DNA damage checkpoint and DNA repair mechanisms play critical roles in the stable maintenance of genetic information. Various forms of DNA damage that arise inside cells due to common errors in normal cellular processes, such as DNA replication, or due to exposure to various DNA damaging agents, must be quickly detected and repaired by checkpoint signaling and repair factors. Telomeres, the natural ends of linear chromosomes, share many features with undesired "broken" DNA, and are recognized and processed by various DNA damage checkpoint and DNA repair proteins. However, their modes of action at telomeres must be altered from their actions at other DNA damage sites to avoid telomere fusions and permanent cell cycle arrest. Interestingly, accumulating evidence indicates that DNA damage checkpoint and DNA repair proteins are essential for telomere maintenance. In this article, we review our current knowledge on various mechanisms by which DNA damage checkpoint and DNA repair proteins are modulated at telomeres and how they might contribute to telomere maintenance in eukaryotes.
MeSH term(s)	Acid Anhydride Hydrolases ; Animals ; DNA Damage ; DNA Repair ; DNA Repair Enzymes/metabolism ; DNA Replication ; DNA-Binding Proteins/metabolism ; Humans ; MRE11 Homologue Protein ; Protein Binding ; Telomerase/metabolism ; Telomere/genetics ; Telomere/metabolism
Chemical Substances	DNA-Binding Proteins ; MRE11 protein, human ; Telomerase (EC 2.7.7.49) ; MRE11 Homologue Protein (EC 3.1.-) ; Acid Anhydride Hydrolases (EC 3.6.-) ; RAD50 protein, human (EC 3.6.-) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2010-06-01
Publishing country	Singapore
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2704569-9
ISSN	2768-6698 ; 2768-6698
ISSN (online)	2768-6698
ISSN	2768-6698
DOI	10.2741/3664
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Article ; Online: A kinase-independent role for the Rad3(ATR)-Rad26(ATRIP) complex in recruitment of Tel1(ATM) to telomeres in fission yeast.

Subramanian, Lakxmi / Nakamura, Toru M

PLoS genetics

2010 Volume 6, Issue 2, Page(s) e1000839

Abstract: ATM and ATR are two redundant checkpoint kinases essential for the stable maintenance of telomeres in eukaryotes. Previous studies have established that MRN (Mre11-Rad50-Nbs1) and ATRIP (ATR Interacting Protein) interact with ATM and ATR, respectively, ... ...

Abstract	ATM and ATR are two redundant checkpoint kinases essential for the stable maintenance of telomeres in eukaryotes. Previous studies have established that MRN (Mre11-Rad50-Nbs1) and ATRIP (ATR Interacting Protein) interact with ATM and ATR, respectively, and recruit their partner kinases to sites of DNA damage. Here, we investigated how Tel1(ATM) and Rad3(ATR) recruitment to telomeres is regulated in fission yeast. Quantitative chromatin immunoprecipitation (ChIP) assays unexpectedly revealed that the MRN complex could also contribute to the recruitment of Tel1(ATM) to telomeres independently of the previously established Nbs1 C-terminal Tel1(ATM) interaction domain. Recruitment of Tel1(ATM) to telomeres in nbs1-c60Delta cells, which lack the C-terminal 60 amino acid Tel1(ATM) interaction domain of Nbs1, was dependent on Rad3(ATR)-Rad26(ATRIP), but the kinase domain of Rad3(ATR) was dispensable. Thus, our results establish that the Rad3(ATR)-Rad26(ATRIP) complex contributes to the recruitment of Tel1(ATM) independently of Rad3(ATR) kinase activity, by a mechanism redundant with the Tel1(ATM) interaction domain of Nbs1. Furthermore, we found that the N-terminus of Nbs1 contributes to the recruitment of Rad3(ATR)-Rad26(ATRIP) to telomeres. In response to replication stress, mammalian ATR-ATRIP also contributes to ATM activation by a mechanism that is dependent on the MRN complex but independent of the C-terminal ATM interaction domain of Nbs1. Since telomere protection and DNA damage response mechanisms are very well conserved between fission yeast and mammalian cells, mammalian ATR-ATRIP may also contribute to the recruitment of ATM to telomeres and to sites of DNA damage independently of ATR kinase activity.
MeSH term(s)	Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Checkpoint Kinase 2 ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/metabolism ; Models, Biological ; Mutation/genetics ; Protein Binding ; Protein Kinases/chemistry ; Protein Kinases/metabolism ; Protein Structure, Tertiary ; Protein Subunits/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Schizosaccharomyces/enzymology ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/metabolism ; Telomere/metabolism
Chemical Substances	Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Nbs1 protein, S pombe ; Protein Subunits ; Schizosaccharomyces pombe Proteins ; rad26 protein, S pombe ; Protein Kinases (EC 2.7.-) ; Checkpoint Kinase 2 (EC 2.7.1.11) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; rad3 protein, S pombe (EC 2.7.11.1) ; tel1 protein, S pombe (EC 2.7.11.1)
Language	English
Publishing date	2010-02-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1000839
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Article ; Online: Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly.

Subramanian, Lakxmi / Toda, Nicholas R T / Rappsilber, Juri / Allshire, Robin C

Open biology

2014 Volume 4, Page(s) 140043

Abstract: CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURP(Scm3), and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURP(Scm3) to ... ...

Abstract	CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURP(Scm3), and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURP(Scm3) to centromeres is cell cycle regulated. Vertebrate Mis18 associates with Mis18BP1(KNL2), which is critical for the recruitment of Mis18 and HJURP(Scm3). We identify two novel fission yeast Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. Eic1 is essential to maintain Cnp1(CENP-A) at centromeres and is crucial for kinetochore integrity; Eic2 is dispensable. Eic1 also associates with Fta7(CENP-Q/Okp1), Cnl2(Nkp2) and Mal2(CENP-O/Mcm21), components of the constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1(KNL2) orthologue has been identified in fission yeast, consequently it remains unknown how the key Cnp1(CENP-A) loading factor Mis18 is recruited. Our findings suggest that Eic1 serves a function analogous to that of Mis18BP1(KNL2), thus representing the functional counterpart of Mis18BP1(KNL2) in fission yeast that connects with a module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated recruitment of the Mis18/Scm3(HJURP) Cnp1(CENP-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.
MeSH term(s)	Amino Acid Sequence ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Centromere/metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/metabolism ; Histone Acetyltransferases/metabolism ; Immunoprecipitation ; Kinetochores/chemistry ; Kinetochores/metabolism ; Molecular Sequence Data ; Mutation ; Protein Binding ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Sequence Alignment
Chemical Substances	CTF19 protein, S cerevisiae ; Carrier Proteins ; Cell Cycle Proteins ; Chromatin ; Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; Cytoskeletal Proteins ; Mis16 protein, S pombe ; Mis18 protein, S pombe ; Mis6 protein, S pombe ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; Histone Acetyltransferases (EC 2.3.1.48) ; histone acetyltransferase type B complex (EC 2.3.1.48)
Language	English
Publishing date	2014-04-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2630944-0
ISSN	2046-2441 ; 2046-2441
ISSN (online)	2046-2441
ISSN	2046-2441
DOI	10.1098/rsob.140043
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Article ; Online: Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket.

Chik, Jennifer K / Moiseeva, Vera / Goel, Pavitra K / Meinen, Ben A / Koldewey, Philipp / An, Sojin / Mellone, Barbara G / Subramanian, Lakxmi / Cho, Uhn-Soo

The Journal of biological chemistry

2019 Volume 294, Issue 38, Page(s) 14119–14134

Abstract: 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 ... ...

Abstract	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
MeSH term(s)	Animals ; Cell Cycle Proteins/metabolism ; Centromere/metabolism ; Centromere Protein A/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomal Proteins, Non-Histone/ultrastructure ; Crystallography, X-Ray/methods ; DNA-Binding Proteins/metabolism ; Dimerization ; Drosophila Proteins/metabolism ; Drosophila Proteins/ultrastructure ; Drosophila melanogaster/metabolism ; Histones/metabolism ; Kinetochores/metabolism ; Kinetochores/ultrastructure ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	CENP-C protein, Drosophila ; Cell Cycle Proteins ; Centromere Protein A ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; Drosophila Proteins ; Histones ; Moa1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; centromere protein C
Language	English
Publishing date	2019-07-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.008464
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Article ; Online: Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly

Lakxmi Subramanian / Nicholas R. T. Toda / Juri Rappsilber / Robin C. Allshire

Open Biology, Vol 4, Iss

2014 Volume 4

Abstract: 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 ... ...

Abstract	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.
Keywords	cenp-a ; centromeres ; epigenetics ; fission yeast ; mis18 ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2014-01-01T00:00:00Z
Publisher	The Royal Society
Document type	Article ; Online
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Article ; Online: Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.

Subramanian, Lakxmi / Medina-Pritchard, Bethan / Barton, Rachael / Spiller, Frances / Kulasegaran-Shylini, Raghavendran / Radaviciute, Guoda / Allshire, Robin C / Arockia Jeyaprakash, A

EMBO reports

2016 Volume 17, Issue 4, Page(s) 496–507

Abstract: 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 ... ...

Abstract	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.
MeSH term(s)	Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Centromere/genetics ; Centromere/physiology ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Epigenesis, Genetic ; 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
Chemical Substances	Carrier Proteins ; Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; DNA-Binding Proteins ; Mis18 protein, S pombe ; Molecular Chaperones ; Schizosaccharomyces pombe Proteins
Language	English
Publishing date	2016-02-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201541520
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Recombination-based telomere maintenance is dependent on Tel1-MRN and Rap1 and inhibited by telomerase, Taz1, and Ku in fission yeast.

Subramanian, Lakxmi / Moser, Bettina A / Nakamura, Toru M

Molecular and cellular biology

2008 Volume 28, Issue 5, Page(s) 1443–1455

Abstract: Fission yeast cells survive loss of the telomerase catalytic subunit Trt1 (TERT) through recombination-based telomere maintenance or through chromosome circularization. Although trt1Delta survivors with linear chromosomes can be obtained, they often ... ...

Abstract	Fission yeast cells survive loss of the telomerase catalytic subunit Trt1 (TERT) through recombination-based telomere maintenance or through chromosome circularization. Although trt1Delta survivors with linear chromosomes can be obtained, they often spontaneously circularize their chromosomes. Therefore, it was difficult to establish genetic requirements for telomerase-independent telomere maintenance. In contrast, when the telomere-binding protein Taz1 is also deleted, taz1Delta trt1Delta cells are able to stably maintain telomeres. Thus, taz1Delta trt1Delta cells can serve as a valuable tool in understanding the regulation of telomerase-independent telomere maintenance. In this study, we show that the checkpoint kinase Tel1 (ATM) and the DNA repair complex Rad32-Rad50-Nbs1 (MRN) are required for telomere maintenance in taz1Delta trt1Delta cells. Surprisingly, Rap1 is also essential for telomere maintenance in taz1Delta trt1Delta cells, even though recruitment of Rap1 to telomeres depends on Taz1. Expression of catalytically inactive Trt1 can efficiently inhibit recombination-based telomere maintenance, but the inhibition requires both Est1 and Ku70. While Est1 is essential for recruitment of Trt1 to telomeres, Ku70 is dispensable. Thus, we conclude that Taz1, TERT-Est1, and Ku70-Ku80 prevent telomere recombination, whereas MRN-Tel1 and Rap1 promote recombination-based telomere maintenance. Evolutionarily conserved proteins in higher eukaryotic cells might similarly contribute to telomere recombination.
MeSH term(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 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
Chemical Substances	Antigens, Nuclear ; DNA-Binding Proteins ; Rap1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Telomere-Binding Proteins ; taz1 protein, S pombe ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; tel1 protein, S pombe (EC 2.7.11.1) ; Telomerase (EC 2.7.7.49) ; Ku Autoantigen (EC 4.2.99.-)
Language	English
Publishing date	2008-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.01614-07
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Article ; Online: Roles of heterochromatin and telomere proteins in regulation of fission yeast telomere recombination and telomerase recruitment.

Khair, Lyne / Subramanian, Lakxmi / Moser, Bettina A / Nakamura, Toru M

The Journal of biological chemistry

2009 Volume 285, Issue 8, Page(s) 5327–5337

Abstract: 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 ... ...

Abstract	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 trt1Delta 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-DeltaT/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-DeltaT/RT to inhibit telomere recombination. However, because loss of Swi6, Clr4, Rad3, Ccq1, or Est1 did not significantly alter the recruitment efficiency of Trt1-DeltaT/RT to telomeres, these factors are likely to enhance the ability of Trt1-DeltaT/RT to inhibit recombination-based survival by contributing to the negative regulation of telomere recombination.
MeSH term(s)	Amino Acid Motifs/physiology ; Amino Acid Sequence ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Checkpoint Kinase 2 ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes, Fungal/genetics ; Chromosomes, Fungal/metabolism ; Gene Deletion ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histone-Lysine N-Methyltransferase ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Recombination, Genetic/physiology ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Sequence Deletion ; Telomerase/genetics ; Telomerase/metabolism ; Telomere/genetics ; Telomere/metabolism ; Telomere-Binding Proteins/genetics ; Telomere-Binding Proteins/metabolism
Chemical Substances	Ccq1 protein, S pombe ; Cell Cycle Proteins ; Chromosomal Proteins, Non-Histone ; Heterochromatin ; Poz1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Swi6 protein, S pombe ; Telomere-Binding Proteins ; taz1 protein, S pombe ; trt1 protein, S pombe ; Methyltransferases (EC 2.1.1.-) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; clr4 protein, S pombe (EC 2.1.1.43) ; Protein Kinases (EC 2.7.-) ; Checkpoint Kinase 2 (EC 2.7.1.11) ; rad3 protein, S pombe (EC 2.7.11.1) ; Telomerase (EC 2.7.7.49)
Language	English
Publishing date	2009-12-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M109.078840
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Article ; Online: Roles of the checkpoint sensor clamp Rad9-Rad1-Hus1 (911)-complex and the clamp loaders Rad17-RFC and Ctf18-RFC in Schizosaccharomyces pombe telomere maintenance.

Khair, Lyne / Chang, Ya-Ting / Subramanian, Lakxmi / Russell, Paul / Nakamura, Toru M

Cell cycle (Georgetown, Tex.)

2010 Volume 9, Issue 11, Page(s) 2237–2248

Abstract: 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 ... ...

Abstract	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.
MeSH term(s)	Alleles ; Carrier Proteins/metabolism ; Carrier Proteins/physiology ; Cell Cycle Proteins/metabolism ; Cell Cycle Proteins/physiology ; Checkpoint Kinase 2 ; DNA/chemistry ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; Endonucleases/metabolism ; Endonucleases/physiology ; Protein Kinases/metabolism ; Protein Kinases/physiology ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Serine-Threonine Kinases/physiology ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism ; Schizosaccharomyces pombe Proteins/physiology ; Telomere/metabolism ; Transcription Factors/metabolism ; Transcription Factors/physiology
Chemical Substances	Carrier Proteins ; Cell Cycle Proteins ; Ctf18 protein, S pombe ; DNA-Binding Proteins ; Rfc1 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Transcription Factors ; hus1 protein, S pombe ; rad9 protein (139691-42-2) ; DNA (9007-49-2) ; Protein Kinases (EC 2.7.-) ; Checkpoint Kinase 2 (EC 2.7.1.11) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; rad3 protein, S pombe (EC 2.7.11.1) ; tel1 protein, S pombe (EC 2.7.11.1) ; Endonucleases (EC 3.1.-) ; rad1 protein, S pombe (EC 3.1.-)
Language	English
Publishing date	2010-06-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.9.11.11920
Database	MEDical Literature Analysis and Retrieval System OnLINE

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