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Journal articles on the topic 'Schizosaccharomyces pombe'

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Published: 4 June 2021
Last updated: 25 May 2024

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1

Davey, John. "Introduction: Schizosaccharomyces pombe." Seminars in Cell Biology 6, no. 2 (April 1995): 53. http://dx.doi.org/10.1016/1043-4682(95)90000-4.

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2

Ekwall, Karl, and Geneviève Thon. "Selecting Schizosaccharomyces pombe Diploids." Cold Spring Harbor Protocols 2017, no. 7 (July 2017): pdb.prot091702. http://dx.doi.org/10.1101/pdb.prot091702.

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3

Tsai, C. S., Ken P. Mitton, and Byron F. Johnson. "Acetate assimilation by the fission yeast, Schizosaccharomyces pombe." Biochemistry and Cell Biology 67, no. 8 (August 1, 1989): 464–67. http://dx.doi.org/10.1139/o89-073.

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The fission yeast Schizosaccharomyces pombe utilizes acetate at subinhibitory concentrations in the presence of D-glucose. The nonionized form of acetate is preferentially utilized, oxidized to 14CO2, and assimilated into lipids and proteins. Acetyl CoA synthetase activity greatly increases in the yeast cells grown in media containing acetate. However, glyoxylate cycle enzymes are not detectable in Schizosaccharomyces pombe. [1-14C] Acetate is incorporated into stereols, sterol esters, neutral lipids, and phospholipids. Assimilation of [1-14C]acetate into the peptide structure of proteins was confirmed by a proteolytic digestion experiment.Key words: acetate utilization, fission yeast, Schizosaccharomyces pombe.
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4

Tohda, Hideki, Yuko Giga-Hama, Kaoru Takegawa, and Hiromichi Kumagai. "Schizosaccharomyces pombe minimum genome factory." Biotechnology and Applied Biochemistry 46, no. 3 (March 1, 2007): 147. http://dx.doi.org/10.1042/ba20060106.

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5

Subramani, S. "Radiation resistance in Schizosaccharomyces pombe." Molecular Microbiology 5, no. 10 (October 1991): 2311–14. http://dx.doi.org/10.1111/j.1365-2958.1991.tb02075.x.

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6

Osothsilp, C., and R. E. Subden. "Malate transport in Schizosaccharomyces pombe." Journal of Bacteriology 168, no. 3 (1986): 1439–43. http://dx.doi.org/10.1128/jb.168.3.1439-1443.1986.

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7

Ekwall, Karl, and Geneviève Thon. "Genetic Analysis of Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2017, no. 8 (August 2017): pdb.top079772. http://dx.doi.org/10.1101/pdb.top079772.

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8

Tohda, H., M. Sasaki, A. Tada, F. Hara, A. Idiris, and H. Kumagai. "Schizosaccharomyces pombe minimum genome factory." Journal of Biotechnology 150 (November 2010): 517–18. http://dx.doi.org/10.1016/j.jbiotec.2010.09.826.

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9

Roguev, Assen, Jiewei Xu, and Nevan J. Krogan. "DNA Preparation from Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2018, no. 1 (July 21, 2017): pdb.prot091959. http://dx.doi.org/10.1101/pdb.prot091959.

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10

Godde, J. S., and J. Widom. "Chromatin structure of Schizosaccharomyces pombe." Journal of Molecular Biology 226, no. 4 (August 1992): 1009–25. http://dx.doi.org/10.1016/0022-2836(92)91049-u.

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11

Gutz, Herbert, and Henning Schmidt. "Switching genes in Schizosaccharomyces pombe." Current Genetics 9, no. 5 (May 1985): 325–31. http://dx.doi.org/10.1007/bf00421601.

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12

Bush, D. A., M. Horisberger, I. Horman, and P. Wursch. "The Wall Structure of Schizosaccharomyces pombe." Microbiology 81, no. 1 (January 1, 2000): 199–206. http://dx.doi.org/10.1099/00221287-81-1-199.

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The wall structure of the fission yeast Schizosaccharomyces pombe, examined by enzymic techniques, consists of a galactomannan, an α-glucan and β-glucan. The structures of the α-glucan and galactomannan were investigated by methylation. The wall structure is discussed in relation to the taxonomic position of the genus Schizosaccharomyces.
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13

Kondrateva, Vera I., and Gennadiy I. Naumov. "POPULATION ANTAGONISM IN THE YEASTS SCHIZOSACCHAROMYCES POMBE." Ecological genetics 9, no. 1 (March 15, 2011): 21–26. http://dx.doi.org/10.17816/ecogen9121-26.

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Using the new yeast Schizosaccharomyces kambucha nom. nud. and genetic lines, widely explored in different laboratories, we continue the investigation of the phenomenon of ascospore death in interstrain hybrids of Sch. pombe. All interstrain hybrids were sterile when analyzed by a micromanipulator. However random spore analysis revealed recombination of control markers, suggesting assignment of the strains studied to the same biological species Sch. pombe. Possible causes of hybrid ascospores death are discussed. The population antagonism of the yeast Sch. pombe should be taken into account in taxonomic studies.
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14

Iwaki, Tomoko, Akira Hosomi, Sanae Tokudomi, Yoko Kusunoki, Yasuko Fujita, Yuko Giga-Hama, Naotaka Tanaka, and Kaoru Takegawa. "Vacuolar protein sorting receptor in Schizosaccharomyces pombe." Microbiology 152, no. 5 (May 1, 2006): 1523–32. http://dx.doi.org/10.1099/mic.0.28627-0.

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The mechanism by which soluble proteins, such as carboxypeptidase Y, reach the vacuole in Saccharomyces cerevisiae is very similar to the mechanism of lysosomal protein sorting in mammalian cells. Vps10p is a receptor for transport of soluble vacuolar proteins in S. cerevisiae. vps10 +, a gene encoding a homologue of S. cerevisiae PEP1/VPS10, has been identified and deleted from the fission yeast Schizosaccharomyces pombe. Deletion of the vps10 + gene resulted in missorting and secretion of Sch. pombe vacuolar carboxypeptidase Cpy1p, indicating that it is required for targeting Cpy1p to the vacuole. Sch. pombe Vps10p (SpVps10p) is a type I transmembrane protein and its C-terminal cytoplasmic tail domain is essential for Cpy1p transport to the vacuole. Cells expressing green fluorescent protein-tagged SpVps10p produced a punctate pattern of fluorescence, indicating that SpVps10p was largely localized in the Golgi compartment. In addition, Sch. pombe vps26 +, vps29 + and vps35 +, encoding homologues of the S. cerevisiae retromer components VPS26, VPS29 and VPS35, were identified and deleted. Fluorescence microscopy demonstrated that SpVps10p mislocalized to the vacuolar membrane in these mutants. These results indicate that the vps26 +, vps29 + and vps35 + gene products are required for retrograde transport of SpVps10p from the prevacuolar compartment back to the Golgi in Sch. pombe cells.
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15

Bischoff, J. R., D. Casso, and D. Beach. "Human p53 inhibits growth in Schizosaccharomyces pombe." Molecular and Cellular Biology 12, no. 4 (April 1992): 1405–11. http://dx.doi.org/10.1128/mcb.12.4.1405-1411.1992.

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Overexpression of wild-type p53 in mammalian cells blocks growth. We show here that the overexpression of wild-type human p53 in the fission yeast Schizosaccharomyces pombe also blocks growth, whereas the overexpression of mutant forms of p53 does not. The p53 polypeptide is located in the nucleus and is phosphorylated at both the cdc2 site and the casein kinase II site in S. pombe. A new dominant mutation of p53, resulting in the change of a cysteine to an arginine at amino acid residue 141, was identified. The results presented here demonstrate that S. pombe could provide a simple system for studying the mechanism of action of human p53.
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16

Bischoff, J. R., D. Casso, and D. Beach. "Human p53 inhibits growth in Schizosaccharomyces pombe." Molecular and Cellular Biology 12, no. 4 (April 1992): 1405–11. http://dx.doi.org/10.1128/mcb.12.4.1405.

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Overexpression of wild-type p53 in mammalian cells blocks growth. We show here that the overexpression of wild-type human p53 in the fission yeast Schizosaccharomyces pombe also blocks growth, whereas the overexpression of mutant forms of p53 does not. The p53 polypeptide is located in the nucleus and is phosphorylated at both the cdc2 site and the casein kinase II site in S. pombe. A new dominant mutation of p53, resulting in the change of a cysteine to an arginine at amino acid residue 141, was identified. The results presented here demonstrate that S. pombe could provide a simple system for studying the mechanism of action of human p53.
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17

Park, Hey-Jung, Jeong-Su Moon, Hong-Gyum Kim, Il-Han Kim, Kanghwa Kim, Eun-Hee Park, and Chang-Jin Lim. "Characterization of a second gene encoding γ-glutamyl transpeptidase from Schizosaccharomyces pombe." Canadian Journal of Microbiology 51, no. 3 (March 1, 2005): 269–75. http://dx.doi.org/10.1139/w04-137.

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The first gene encoding γ-glutamyl transpeptidase (GGTI) of the fission yeast has previously been characterized, and its expression was found to be regulated by various oxidative stress-inducing agents. In this work, a second gene, encoding GGTII, was cloned and characterized from the fission yeast Schizosaccharomyces pombe. The structural gene encoding GGTII was amplified from the genomic DNA of the fission yeast and ligated into the shuttle vector pRS316 to generate the recombinant plasmid pPHJ02. The determined sequence contains 3040 bp and is able to encode the putative 611 amino acid sequence of GGTII, which resembles the counterparts of Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus, and Escherichia coli. The DNA sequence also contains 940-bp upstream and 289-bp downstream regions of the GGTII gene. The Schizosaccharomyces pombe cells harboring plasmid pPHJ02 showed about 4-fold higher GGT activity in the exponential phase than the cells harboring the vector only, indicating that the cloned GGTII gene is functional. The S. pombe cells containing the cloned GGTII gene were found to contain higher levels of both intracellular glutathione (GSH) content and GSH uptake. The S. pombe cells harboring plasmid pPHJ02 showed increased survival on solid media containing hydrogen peroxide, diethylmaleate, aluminum chloride, cadmium chloride, or mercuric chloride. The GGTII mRNA level was significantly elevated by treatment with GSH-depleting diethylmaleate. These results imply that the S. pombe GGTII gene produces functional GGTII protein and is involved in the response to oxidative stresses in S. pombe cells.Key words: fission yeast, genomic DNA, γ-glutamyl transpeptidase, regulation, Schizosaccharomyces pombe, stress response.
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18

MOHAPATRA, BANDITA. "Antifungal Activity of ZnO Nanobullets against Schizosaccharomyces pombe." Asian Journal of Chemistry 35, no. 9 (August 31, 2023): 2247–55. http://dx.doi.org/10.14233/ajchem.2023.28226.

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In this study, an enhanced antifungal response of ZnO nanobullets (NBs) against Schizosaccharomyces pombe is reported. The ZnO NBs were prepared by alkali precipitation method and confirmed by microscopic, morphological and optical studies using SEM, EDX, TEM, HRTEM and photoluminescence (PL) spectroscopic techniques. Growth kinetics and MIC studies were conducted following the growth inhibition percentage studies. Colony forming assay, well diffusion, disc diffusion, N-acetyl cysteine (NAC) effect on S. pombe growth, trypan blue study, cellular reactive oxygen species (ROS) quantification using H2DCFDA dye, Bradford assay, DNA fragmentation and all other relevant protocols were performed in antifungal studies. ZnO nanobullets (NBs) were shown by SEM and TEM examinations to have an average size of 50 nm. The hexagonal wurtzite structure of ZnO NBs was confirmed by HRTEM’s lattice fringe findings. Defectrelated visible emissions at 412, 436, 457 and 564 nm were confirmed via PL analysis. It was found that ZnO NBs resulted in complete growth inhibition of S. pombe at 200 μg/mL. When S. pombe was treated with ZnO NBs, the Bradford assay revealed enhanced protein leakage, but the TBARS assay revealed lipid peroxidation brought on by reactive oxygen species (ROS). When S. pombe was exposed to ZnO NBs, the H2DCFDA assay revealed increased ROS generation, whilst the trypan blue assay revealed increased cell membrane fusion and lower viability. According to present study, the treatment with ZnO NBs caused S. pombe to develop damaged cell walls, leaky proteins and DNA breakage.
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19

Wixon, Jo. "Featured Organism: Schizosaccharomyces pombe, The Fission Yeast." Comparative and Functional Genomics 3, no. 2 (2002): 194–204. http://dx.doi.org/10.1002/cfg.92.

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Schizosaccharomyces pombe, the fission yeast, has long been a crucial model for the study of the eukaryote cell cycle. We take a look at this important yeast, whose genome has recently been completed, featuring comments from Valerie Wood, Jürg Bähler, Ramsay McFarlane, Susan Forsburg, Iain Hagan and Paul Nurse on the implications of having the complete sequence and future prospects for pombe genomics.
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20

Smith, J. G., M. S. Caddle, G. H. Bulboaca, J. G. Wohlgemuth, M. Baum, L. Clarke, and M. P. Calos. "Replication of centromere II of Schizosaccharomyces pombe." Molecular and Cellular Biology 15, no. 9 (September 1995): 5165–72. http://dx.doi.org/10.1128/mcb.15.9.5165.

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The centromeric DNAs of Schizosaccharomyces pombe chromosomes resemble those of higher eukaryotes in being large and composed predominantly of repeated sequences. To begin a detailed analysis of the mode of replication of a complex centromere, we examined whether any sequences within S. pombe centromere II (cen2) have the ability to mediate autonomous replication. We found a high density of segments with such activity, including at least eight different regions comprising most of the repeated and unique centromeric DNA elements. A physical mapping analysis using two-dimensional gels showed that autonomous replication initiated within the S. pombe sequences in each plasmid. A two-dimensional gel analysis of replication on the chromosomes revealed that the K and L repeat elements, which occur in multiple copies at all three centromeres and comprise approximately 70% of total centromeric DNA mass in S. pombe, are both sites of replication initiation. In contrast, the unique cen2 central core, which contains multiple segments that can support autonomous replication, appears to be repressed for initiation on the chromosome. We discuss the implications of these findings for our understanding of DNA replication and centromere function.
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21

Armstrong, John, Alison Pidoux, Sally Bowden, Mark Craighead, Neil Bone, and Everton Robinson. "The ypt proteins of Schizosaccharomyces pombe." Biochemical Society Transactions 22, no. 2 (May 1, 1994): 460–63. http://dx.doi.org/10.1042/bst0220460.

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22

Wood, V., R. Gwilliam, M. A. Rajandream, M. Lyne, R. Lyne, A. Stewart, J. Sgouros, et al. "The genome sequence of Schizosaccharomyces pombe." Nature 415, no. 6874 (February 21, 2002): 871–80. http://dx.doi.org/10.1038/nature724.

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23

O’Donoghue, Jean E., Dawadschargal Bech-Otschir, Ida B. Larsen, Mairi Wallace, Rasmus Hartmann-Petersen, and Colin Gordon. "Nedd8 processing enzymes in Schizosaccharomyces pombe." BMC Biochemistry 14, no. 1 (2013): 8. http://dx.doi.org/10.1186/1471-2091-14-8.

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24

Sayers, Lee G., Satoshi Katayama, Kentaro Nakano, Harry Mellor, Issei Mabuchi, Takashi Toda, and Peter J. Parker. "Rho-dependence of Schizosaccharomyces pombe Pck2." Genes to Cells 5, no. 1 (January 2000): 17–27. http://dx.doi.org/10.1046/j.1365-2443.2000.00301.x.

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25

Pei, Y. "Characterization of Schizosaccharomyces pombe RNA triphosphatase." Nucleic Acids Research 29, no. 2 (January 15, 2001): 387–96. http://dx.doi.org/10.1093/nar/29.2.387.

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26

Bah, Amadou, Harry Wischnewski, Vadim Shchepachev, and Claus M. Azzalin. "The telomeric transcriptome of Schizosaccharomyces pombe." Nucleic Acids Research 40, no. 7 (December 1, 2011): 2995–3005. http://dx.doi.org/10.1093/nar/gkr1153.

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27

Grallert, Agnes, and Iain M. Hagan. "Elementary Protein Analysis in Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2017, no. 3 (March 2017): pdb.top079806. http://dx.doi.org/10.1101/pdb.top079806.

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28

Hagan, Iain M., and Steven Bagley. "Fixed-Cell Imaging of Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2016, no. 7 (July 2016): pdb.top079830. http://dx.doi.org/10.1101/pdb.top079830.

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29

Cam, Hugh P., and Simon Whitehall. "Analysis of Heterochromatin in Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2016, no. 11 (November 2016): pdb.top079889. http://dx.doi.org/10.1101/pdb.top079889.

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30

GOULD, K. "Protocols for experimentation with Schizosaccharomyces pombe." Methods 33, no. 3 (July 2004): 187–88. http://dx.doi.org/10.1016/j.ymeth.2003.11.012.

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31

SIAM, R. "Choosing and using Schizosaccharomyces pombe plasmids." Methods 33, no. 3 (July 2004): 189–98. http://dx.doi.org/10.1016/j.ymeth.2003.11.013.

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32

Moser, Bettina A., and Paul Russell. "Cell cycle regulation in Schizosaccharomyces pombe." Current Opinion in Microbiology 3, no. 6 (December 2000): 631–36. http://dx.doi.org/10.1016/s1369-5274(00)00152-1.

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33

Kuramae, Eiko E., Vincent Robert, Berend Snel, and Teun Boekhout. "Conflicting phylogenetic position of Schizosaccharomyces pombe." Genomics 88, no. 4 (October 2006): 387–93. http://dx.doi.org/10.1016/j.ygeno.2006.07.001.

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34

Andreadis, Christos, and Jilong Liu. "Cytoophidium-forming proteins in Schizosaccharomyces pombe." Mechanisms of Development 145 (July 2017): S129. http://dx.doi.org/10.1016/j.mod.2017.04.356.

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35

Jimenez, J. "Cryopreservation of competent Schizosaccharomyces pombe protoplasts." Trends in Genetics 7, no. 2 (February 1991): 40. http://dx.doi.org/10.1016/0168-9525(91)90226-g.

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36

Manna, Filomena, Domenica Rita Massardo, Luigi Del Giudice, Aniello Buonocore, Anno Giulia Nappo, Pietro Alifano, Bernd Schäfer, and Klaus Wolf. "The mitochondrial genome of Schizosaccharomyces pombe." Current Genetics 19, no. 4 (April 1991): 295–99. http://dx.doi.org/10.1007/bf00355058.

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37

LIU, Yu-Ling. "Characterization of Schizosaccharomyces pombe secreted proteins." HEREDITAS 29, no. 02 (2007): 250. http://dx.doi.org/10.1360/yc-007-0250.

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38

Gu, Weiwei, Laurence D. Etkin, Mark A. Le Gros, and Carolyn A. Larabell. "X-ray tomography of Schizosaccharomyces pombe." Differentiation 75, no. 6 (July 2007): 529–35. http://dx.doi.org/10.1111/j.1432-0436.2007.00180.x.

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39

Zhou, Lihong, and Felicity Z. Watts. "Nep1, a Schizosaccharomyces pombe deneddylating enzyme." Biochemical Journal 389, no. 2 (July 5, 2005): 307–14. http://dx.doi.org/10.1042/bj20041991.

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Nedd8 is a ubiquitin-like modifier that is attached to the cullin components of E3 ubiquitin ligases. More recently, p53 has also been shown to be Nedd8-modified. Nedd8 attachment occurs in a manner similar to that observed for other ubiquitin-like modifiers. In the present study, we report on the characterization of Nep1, a deneddylating enzyme in fission yeast (Schizosaccharomyces pombe). Unlike loss of ned8, deletion of the nep1 gene is not lethal, although nep1.d cells are heterogeneous in length, suggesting a defect in cell-cycle progression. Viability of nep1.d cells is dependent on a functional spindle checkpoint but not on the DNA integrity checkpoint. Deletion of a related gene (nep2), either alone or in combination with nep1.d, also has little effect on cell viability. We show that Nep1 can deneddylate the Pcu1, Pcu3 and Pcu4 cullins in vitro and that its activity is sensitive to N-ethylmaleimide, consistent with the idea that it is a member of the cysteine protease family. nep1.d cells accumulate Nedd8-modified proteins, although these do not correspond to modified forms of the cullins, suggesting that, although Nep1 can deneddylate cullins in vitro, this is not its main function in vivo. Nep1 can be co-precipitated with the signalosome subunit Csn5. Nep1 itself is present in a high-molecular-mass complex, but the presence of this complex is not dependent on the production of intact signalosomes. Our results suggest that, in vivo, Nep1 may be responsible for deneddylating proteins other than cullins.
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40

Cam, Hugh P., and Simon Whitehall. "Chromatin Immunoprecipitation (ChIP) in Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2016, no. 11 (November 2016): pdb.prot091546. http://dx.doi.org/10.1101/pdb.prot091546.

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41

Ekwall, Karl, and Geneviève Thon. "Setting up Schizosaccharomyces pombe Crosses/Matings." Cold Spring Harbor Protocols 2017, no. 7 (July 2017): pdb.prot091694. http://dx.doi.org/10.1101/pdb.prot091694.

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42

Ekwall, Karl, and Geneviève Thon. "Mating-Type Determination in Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2017, no. 8 (August 2017): pdb.prot091728. http://dx.doi.org/10.1101/pdb.prot091728.

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43

Ekwall, Karl, and Geneviève Thon. "Ethyl Methanesulfonate Mutagenesis in Schizosaccharomyces pombe." Cold Spring Harbor Protocols 2017, no. 8 (August 2017): pdb.prot091736. http://dx.doi.org/10.1101/pdb.prot091736.

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44

Kuhn, Andreas N., and Norbert F. Käufer. "Pre-mRNA splicing in Schizosaccharomyces pombe." Current Genetics 42, no. 5 (December 13, 2002): 241–51. http://dx.doi.org/10.1007/s00294-002-0355-2.

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45

Rowley, R., S. Subramani, and P. G. Young. "Checkpoint controls in Schizosaccharomyces pombe: rad1." EMBO Journal 11, no. 4 (April 1992): 1335–42. http://dx.doi.org/10.1002/j.1460-2075.1992.tb05178.x.

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46

Bentley, N. J., D. A. Holtzman, G. Flaggs, K. S. Keegan, A. DeMaggio, J. C. Ford, M. Hoekstra, and A. M. Carr. "The Schizosaccharomyces pombe rad3 checkpoint gene." EMBO Journal 15, no. 23 (December 1996): 6641–51. http://dx.doi.org/10.1002/j.1460-2075.1996.tb01054.x.

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47

Gutz, H., P. Kapitza, and L. K�ster. "Stable h + strains of Schizosaccharomyces pombe." Naturwissenschaften 73, no. 4 (April 1986): 209–10. http://dx.doi.org/10.1007/bf00417726.

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48

Chappell, T. G., and G. Warren. "A galactosyltransferase from the fission yeast Schizosaccharomyces pombe." Journal of Cell Biology 109, no. 6 (December 1, 1989): 2693–702. http://dx.doi.org/10.1083/jcb.109.6.2693.

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A membrane-associated galactosyltransferase has been purified to homogeneity from the fission yeast, Schizosaccharomyces pombe. The enzyme has a molecular weight of 61,000 and is capable of transfering galactose from UDP-galactose (UDP-Gal) to a variety of mannose-based acceptors to form an alpha-1,2 galactosyl mannoside linkage. Immunofluorescence localization of the protein is consistent with the presence of the enzyme in the Golgi apparatus of S. pombe. This, together with the presence of terminal, alpha-linked galactose on the N-linked oligosaccharides of S. pombe secretory proteins, suggests that the galactosyltransferase is an enzyme involved in the processing of glycoproteins transported through the Golgi apparatus in fission yeast.
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49

Park, Hey-Jung, Hye-Won Lim, Kanghwa Kim, Il-Han Kim, Eun-Hee Park, and Chang-Jin Lim. "Characterization and regulation of the γ-glutamyl transpeptidase gene from the fission yeast Schizosaccharomyces pombe." Canadian Journal of Microbiology 50, no. 1 (January 1, 2004): 61–67. http://dx.doi.org/10.1139/w03-106.

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The structural gene for the putative γ-glutamyl transpeptidase (GGT) was isolated from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The determined sequence contained 3324 bp and encoded the predicted 630 amino acid sequence of GGT, which resembles counterparts in Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae, and Escherichia coli. The S. pombe cells harboring the cloned GGT gene showed about twofold higher GGT activity in the exponential phase than the cells harboring the vector only, indicating that the cloned GGT gene was functional. To monitor the expression of the S. pombe GGT gene, we fused the fragment 1085 bp upstream of the cloned GGT gene into the promoterless β-galactosidase gene of the shuttle vector YEp367R to generate the fusion plasmid pGT98. The synthesis of β-galactosidase from the fusion plasmid in S. pombe cells was enhanced by treatments with NO-generating sodium nitroprusside (SN), L-buthionine-(S,R)-sulfoximine (BSO), and glycerol. The GGT mRNA level in the S. pombe cells was increased by SN and BSO. Involvement of Pap1 in the induction of the GGT gene by SN and BSO was observed.Key words: fission yeast, genomic DNA, γ-glutamyl transpeptidase, Pap1, regulation, Schizosaccharomyces pombe.
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50

Rasmussen, Colin, and Christine Wiebe. "Cloning of aSchizosaccharomyces pombehomologue of elongation factor 1 alpha by two-hybrid selection of calmodulin-binding proteins." Biochemistry and Cell Biology 77, no. 5 (October 1, 1999): 421–30. http://dx.doi.org/10.1139/o99-055.

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Abstract:
This study reports the cloning and characterization of a cDNA encoding elongation factor 1-alpha (EF1alpha) from the yeast Schizosaccharomyces pombe. The cDNA was cloned from an Schizosaccharomyces pombe expression library by a two-hybrid selection for clones encoding calmodulin (CaM)-binding proteins. The predicted protein is highly homologous to mammalian EF1alpha, indicating a strong tendency towards conservation of the primary amino acid sequence. The protein was expressed as a glutathione S-transferase fusion in both bacteria and in Schizosaccharomyces pombe. The bacterial protein was shown by solution assay to compete with CaM kinase II for CaM. The CaM binding domain was localized to the C-terminus of the protein by this method. Expression of full-length EF1alpha in vivo caused an increase in cell cycle length and a decreased rate of growth as evidenced by a lack of elongated cells in slowly dividing cultures. This effect appears to involve CaM binding because a truncation mutant version of EF1alpha lacking the CaM binding domain did not cause cell cycle delay.Key words: calmodulin, two-hybrid selection, calmodulin-binding protein, yeast, cell proliferation.
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