| Satoshi Okada | Last modified date：2023.11.22 |
Assistant Professor /
Department of Basic Medicine /
Faculty of Medical Sciences
Papers
| 1. | Goro Doi, Satoshi Okada, Takehiro Yasukawa, Yuki Sugiyama, Siqin Bala, Shintaro Miyazaki, Dongchon Kang, Takashi Ito, Catalytically inactive Cas9 impairs DNA replication fork progression to induce focal genomic instability., Nucleic Acids Research, 10.1093/nar/gkaa1241, 2021.01, Catalytically inactive Cas9 (dCas9) has become an increasingly popular tool for targeted gene activation/inactivation, live-cell imaging, and base editing. While dCas9 was reported to induce base substitutions and indels, it has not been associated with structural variations. Here, we show that dCas9 impedes replication fork progression to destabilize tandem repeats in budding yeast. When targeted to the CUP1 array comprising ∼16 repeat units, dCas9 induced its contraction in most cells, especially in the presence of nicotinamide. Replication intermediate analysis demonstrated replication fork stalling in the vicinity of dCas9-bound sites. Genetic analysis indicated that while destabilization is counteracted by the replisome progression complex components Ctf4 and Mrc1 and the accessory helicase Rrm3, it involves single-strand annealing by the recombination proteins Rad52 and Rad59. Although dCas9-mediated replication fork stalling is a potential risk in conventional applications, it may serve as a novel tool for both mechanistic studies and manipulation of genomic instability.. |
| 2. | Younghoon Oh, Jennifer H. Schreiter, Hiroki Okada, Carsten Wloka, Satoshi Okada, Di Yan, Xudong Duan, Erfei Bi, Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis, Current Biology, 10.1016/j.cub.2017.08.032, 27, 18, 2878-2886.e5, 2017.09, Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1–14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example the FtsZ ring in bacteria [15], the phragmoplast in plants [16], and the actomyosin ring in fungi and animals [17, 18]. Although the cytoskeletal structures have been analyzed extensively, the mechanisms of ECM remodeling remain poorly understood. In the budding yeast Saccharomyces cerevisiae, ECM remodeling refers to sequential formations of the primary and secondary septa that are catalyzed by chitin synthase-II (Chs2) and chitin synthase-III (the catalytic subunit Chs3 and its activator Chs4), respectively [18, 19]. Surprisingly, both Chs2 and Chs3 are delivered to the division site at the onset of cytokinesis [6, 20]. What keeps Chs3 inactive until secondary septum formation remains unknown. Here, we show that Hof1 binds to the Sel1-like repeats (SLRs) of Chs4 via its F-BAR domain and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23]. ECM remodeling during cytokinesis occurs in a spatiotemporally controlled manner. Oh et al. report that the F-BAR protein Hof1 interacts with the SLR protein Chs4 to ensure that secondary septum formation occurs after actomyosin ring constriction and primary septum formation during cytokinesis in budding yeast.. |
| 3. | Younghoon Oh, Jennifer H. Schreiter, Hiroki Okada, Carsten Wloka, Satoshi Okada, Di Yan, Xudong Duan, Erfei Bi, Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis, CURRENT BIOLOGY, 10.1016/j.cub.2017.08.032, 27, 18, 2878-+, 2017.09, Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1-14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example the FtsZ ring in bacteria [15], the phragmoplast in plants [16], and the actomyosin ring in fungi and animals [17, 18]. Although the cytoskeletal structures have been analyzed extensively, the mechanisms of ECM remodeling remain poorly understood. In the budding yeast Saccharomyces cerevisiae, ECM remodeling refers to sequential formations of the primary and secondary septa that are catalyzed by chitin synthase-II (Chs2) and chitin synthase-III (the catalytic subunit Chs3 and its activator Chs4), respectively [18, 19]. Surprisingly, both Chs2 and Chs3 are delivered to the division site at the onset of cytokinesis [6, 20]. What keeps Chs3 inactive until secondary septum formation remains unknown. Here, weshow that Hof1 binds to the Sel1-like repeats (SLRs) of Chs4 via its F-BAR domain and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23].. |
| 4. | Satoshi Okada, C. Wloka, E. Bi, Analysis of protein dynamics during cytokinesis in budding yeast, Methods in Cell Biology, 10.1016/bs.mcb.2016.04.002, 2017.01, Cytokinesis is essential for development and survival of all organisms by increasing cell number and diversity. It is a highly regulated process that requires spatiotemporal coordination of hundreds of proteins functioning in the assembly, constriction, and disassembly of a contractile actomyosin ring, targeted vesicle fusion, and localized extracellular matrix remodeling. Cytokinesis has been studied in multiple systems with a wide range of technologies to learn the common principles. In this chapter, we describe the analysis of protein dynamics during cytokinesis in the budding yeast. Saccharomyces cerevisiae by several live-cell imaging methods. This, in combination with the power of yeast genetics, has yielded novel insights into the mechanism of cytokinesis. Similar approaches are increasingly used to study this fundamental process in more complex systems.. |
| 5. | Satoshi Okada, Mid Eum Lee, Erfei Bi, Hay Oak Park, Probing Cdc42 Polarization Dynamics in Budding Yeast Using a Biosensor, Methods in Enzymology, 10.1016/bs.mie.2017.01.011, 589, 171-190, 2017.01, Cdc42 is a small guanosine triphosphatase (GTPase) that plays a central role in polarity development in diverse cell types. Since the activity of Cdc42 is dynamically controlled in time and space, it is required to develop a biosensor to monitor its activation in vivo. In this chapter, we describe the construction and usage of a simple and robust biosensor for monitoring active Cdc42 in budding yeast. This affinity-based biosensor uses a red fluorescent protein fused to a Cdc42- and Rac-interactive binding motif from one of the Cdc42 effector proteins. Because it binds specifically to the GTP-bound Cdc42, this biosensor can be used to monitor Cdc42 activation in vivo. This or similar biosensors can be widely used for studying GTPase signaling in other cell types because of the conserved CRIB motif present among GTPase targets.. |
| 6. | Keiji Kito, Mitsuhiro Okada, Yuko Ishibashi, Satoshi Okada, Takashi Ito, A strategy for absolute proteome quantification with mass spectrometry by hierarchical use of peptide-concatenated standards, Proteomics, 10.1002/pmic.201500414, 16, 10, 1457-1473, 2016.05, The accurate and precise absolute abundance of proteins can be determined using mass spectrometry by spiking the sample with stable isotope-labeled standards. In this study, we developed a strategy of hierarchical use of peptide-concatenated standards (PCSs) to quantify more proteins over a wider dynamic range. Multiple primary PCSs were used for quantification of many target proteins. Unique "ID-tag peptides" were introduced into individual primary PCSs, allowing us to monitor the exact amounts of individual PCSs using a "secondary PCS" in which all "ID-tag peptides" were concatenated. Furthermore, we varied the copy number of the "ID-tag peptide" in each PCS according to a range of expression levels of target proteins. This strategy accomplished absolute quantification over a wider range than that of the measured ratios. The quantified abundance of budding yeast proteins showed a high reproducibility for replicate analyses and similar copy numbers per cell for ribosomal proteins, demonstrating the accuracy and precision of this strategy. A comparison with the absolute abundance of transcripts clearly indicated different post-transcriptional regulation of expression for specific functional groups. Thus, the approach presented here is a faithful method for the absolute quantification of proteomes and provides insights into biological mechanisms, including the regulation of expressed protein abundance.. |
| 7. | Keiji Kito, Mitsuhiro Okada, Yuko Ishibashi, Satoshi Okada, Takashi Ito, A strategy for absolute proteome quantification with mass spectrometry by hierarchical use of peptide‐concatenated standards, Proteomics, 10.1002/pmic.201500414, 16, 10, 1457-1473, 2016.05. |
| 8. | Zhonghui Feng, Satoshi Okada, Guoping Cai, Bing Zhou, Erfei Bi, Myosin‑II heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis, Molecular Biology of the Cell, 10.1091/mbc.E14-09-1363, 26, 7, 1211-1224, 2015.04, MLC1 is a haploinsufficient gene encoding the essential light chain for Myo1, the sole myosin‑II heavy chain in the budding yeast Saccharomyces cerevisiae. Mlc1 defines an essential hub that coordinates actomyosin ring function, membrane trafficking, and septum formation during cytokinesis by binding to IQGAP, myosin‑II, and myosin‑V. However, the mechanism of how Mlc1 is targeted to the division site during the cell cycle remains unsolved. By constructing a GFP‑tagged MLC1 under its own promoter control and using quantitative live‑cell imaging coupled with yeast mutants, we found that septin ring and actin filaments mediate the targeting of Mlc1 to the division site before and during cytokinesis, respectively. Both mechanisms contribute to and are collectively required for the accumulation of Mlc1 at the division site during cytokinesis. We also found that Myo1 plays a major role in the septin‑dependent Mlc1 localization before cytokinesis, whereas the formin Bni1 plays a major role in the actin filament-dependent Mlc1 localization during cytokinesis. Such a two‑tiered mechanism for Mlc1 localization is presumably required for the ordered assembly and robustness of cytokinesis machinery and is likely conserved across species.. |
| 9. | Zhonghui Feng, Satoshi Okada, Guoping Cai, Bing Zhou, Erfei Bi, Myosin‑II heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis, Molecular biology of the cell, 10.1091/mbc.E14-09-1363, 26, 7, 1211-1224, 2015.04. |
| 10. | Katy Ong, Carsten Wloka, Satoshi Okada, Tatyana Svitkina, Erfei Bi, Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle, NATURE COMMUNICATIONS, 10.1038/ncomms6698, 5, 5698, 2014.12, Septins perform diverse functions through the formation of filaments and higher-order structures. However, the exact architecture of septin structures remains unclear. In the budding yeast Saccharomyces cerevisiae, septins form an 'hourglass' at the mother-bud neck before cytokinesis, which is converted into a 'double ring' during cytokinesis. Here, using platinum-replica electron microscopy, we find that the early hourglass consists of septin double filaments oriented along the mother-bud axis. In the late hourglass, these double filaments are connected by periodic circumferential single filaments on the membrane-proximal side and are associated with centrally located, circumferential, myosin-II thick filaments on the membrane-distal side. The double ring consists of exclusively circumferential septin filaments. Live-cell imaging studies indicate that the hourglass-to-double ring transition is accompanied by loss of septin subunits from the hourglass and reorganization of the remaining subunits into the double ring. This work provides an unparalleled view of septin structures within cells and defines their remodelling dynamics during the cell cycle.. |
| 11. | Katy Ong, Carsten Wloka, Satoshi Okada, Tatyana Svitkina, Erfei Bi, Architecture and dynamic remodelling of the septin cytoskeleton during the cell cycle, Nature Communications, 10.1038/ncomms6698, 5, 2014.01, Septins perform diverse functions through the formation of filaments and higher-order structures. However, the exact architecture of septin structures remains unclear. In the budding yeast Saccharomyces cerevisiae, septins form an 'hourglass' at the mother-bud neck before cytokinesis, which is converted into a 'double ring' during cytokinesis. Here, using platinum-replica electron microscopy, we find that the early hourglass consists of septin double filaments oriented along the mother-bud axis. In the late hourglass, these double filaments are connected by periodic circumferential single filaments on the membrane-proximal side and are associated with centrally located, circumferential, myosin-II thick filaments on the membrane-distal side. The double ring consists of exclusively circumferential septin filaments. Live-cell imaging studies indicate that the hourglass-to-double ring transition is accompanied by loss of septin subunits from the hourglass and reorganization of the remaining subunits into the double ring. This work provides an unparalleled view of septin structures within cells and defines their remodelling dynamics during the cell cycle.. |
| 12. | Marcin Leda, Satoshi Okada, Erfei Bi, Yves Barral, Andrew B. Goryachev, Particle-Based model of cellular morphogenesis in budding yeast, 3rd International Conference on Particle-Based Methods Fundamentals and Applications, Particles 2013 Particle-Based Methods III: Fundamentals and Applications - Proceedings of the 3rd International Conference on Particle-based MethodsFundamentals and Applications, Particles 2013, 145-152, 2013.09, We apply Lagrangian particle method combined with the level-set method to model morphogenesis of budding yeast on the subcellular level. We model the biochemical reactions, anisotropic diffusion, membrane-cytoplasmic transport of proteins and introduction of new membrane material (exocytosis) that occur on the plasma membrane. Exocytosis results in protrusion of the membrane surface. Hence, to model these phenomena we need to solve a system of reaction-diffusion-advection equations on the evolving surface.. |
| 13. | Satoshi Okada, Marcin Leda, Julia Hanna, Natasha S. Savage, Andrew B. Goryachev, Erfei Bi, Interplay between Cdc42 activity, septins, and exocytosis shapes septin ring in yeast, YEAST, 30, 112-112, 2013.09. |
| 14. | Taichi Umeyama, Satoshi Okada, Takashi Ito, Synthetic gene circuit-mediated monitoring of endogenous metabolites Identification of GAL11 as a novel multicopy enhancer of S-adenosylmethionine level in yeast, ACS Synthetic Biology, 10.1021/sb300115n, 2, 8, 425-430, 2013.08, Monitoring levels of key metabolites in living cells comprises a critical step in various investigations. The simplest approach to this goal is a fluorescent reporter gene using an endogenous promoter responsive to the metabolite. However, such a promoter is often not identified or even present in the species of interest. An alternative can be a synthetic gene circuit based on a heterologous pair consisting of a promoter and a transcription factor known to respond to the metabolite. We exploited the met operator and MetJ repressor of Escherichia coli, the interaction between which depends on S-adenosylmethionine (SAM), to construct synthetic gene circuits that report SAM levels in Saccharomyces cerevisiae. Using a dual-input circuit that outputs selection marker genes in a doxycycline-tunable manner, we screened a genomic library to identify GAL11 as a novel multicopy enhancer of SAM levels. These results demonstrate the potential and utility of synthetic gene circuit-mediated metabolite monitoring.. |
| 15. | Taichi Umeyama, Satoshi Okada, Takashi Ito, Synthetic Gene Circuit-Mediated Monitoring of Endogenous Metabolites: Identification of GAL11 as a Novel Multicopy Enhancer of S-Adenosylmethionine Level in Yeast, ACS SYNTHETIC BIOLOGY, 10.1021/sb300115n, 2, 8, 425-430, 2013.08, Monitoring levels of key metabolites in living cells comprises a critical step in various investigations. The simplest approach to this goal is a fluorescent reporter gene using an endogenous promoter responsive to the metabolite. However, such a promoter is often not identified or even present in the species of interest. An alternative can be a synthetic gene circuit based on a heterologous pair consisting of a promoter and a transcription factor known to respond to the metabolite. We exploited the met operator and MetJ repressor of Escherichia coli, the interaction between which depends on S-adenosylmethionine (SAM), to construct synthetic gene circuits that report SAM levels in Saccharomyces cerevisiae. Using a dual-input circuit that outputs selection marker genes in a doxycycline-tunable manner, we screened a genomic library to identify GAL11 as a novel multicopy enhancer of SAM levels. These results demonstrate the potential and utility of synthetic gene circuit-mediated metabolite monitoring.. |
| 16. | Daughter cell identity emerges from the interplay of Cdc42, septins, and exocytosis.. |
| 17. | Satoshi Okada, Marcin Leda, Julia Hanna, Natasha S. Savage, Erfei Bi, Andrew B. Goryachev, Daughter Cell Identity Emerges from the Interplay of Cdc42, Septins, and Exocytosis, Developmental Cell, 10.1016/j.devcel.2013.06.015, 26, 2, 148-161, 2013.07, Asymmetric cell division plays a crucial role in cell differentiation, unequal replicative senescence, and stem cell maintenance. In budding yeast, the identities of mother and daughter cells begin to diverge at bud emergence when distinct plasma-membrane domains are formed and separated by a septin ring. However, the mechanisms underlying this transformation remain unknown. Here, we show that septins recruited to the site of polarization by Cdc42-GTP inhibit Cdc42 activity in a negative feedback loop, and this inhibition depends on Cdc42 GTPase-activating proteins. Combining live-cell imaging and computational modeling, we demonstrate that the septin ring is sculpted by polarized exocytosis, which creates a hole in the accumulating septin density and relieves the inhibition of Cdc42. The nascent ring generates a sharp boundary that confines the Cdc42 activity and exocytosis strictly to its enclosure and thus clearly delineates the daughter cell identity. Our findings define a fundamental mechanism underlying eukaryotic cell fate differentiation.. |
| 18. | Satoshi Okada, Marcin Leda, Julia Hanna, Natasha S Savage, Erfei Bi, Andrew B Goryachev, Daughter cell identity emerges from the interplay of Cdc42, septins, and exocytosis, Developmental cell, 10.1016/j.devcel.2013.06.015, 26, 2, 148-161, 2013.07. |
| 19. | Satoshi Okada, Kazuhisa Ota, Takashi Ito, Circular permutation of ligand-binding module improves dynamic range of genetically encoded FRET-based nanosensor, Protein Science, 10.1002/pro.266, 18, 12, 2518-2527, 2009.12, Quantitative measurement of small molecules with high spatiotemporal resolution provides a solid basis for correct understanding and accurate modeling of metabolic regulation. A promising approach toward this goal is the FLIP (fluorescent indicator protein) nanosensor based on bacterial periplasmic binding proteins (PBPs) and fluorescence resonance energy transfer (FRET) between the yellow and cyan variants of green fluorescent protein (GFP). Each FLIP has a PBP module that specifically binds its ligand to induce a conformation change, leading to a change in FRET between the two GFP variant modules attached to the N- and C-termini of the PBP. The larger is the dynamic range the more reliable is the measurement. Thus, we attempted to expand the dynamic range of FLIP by introducing a circular permutation with a hinge loop deletion to the PBP module. All the six circularly permutated PBPs tested, including structurally distinct Type I and Type II PBPs, showed larger dynamic ranges than their respective native forms when used for FLIP. Notably, the circular permutation made three PBPs, which totally failed to show FRET change when used as their native forms, fully capable of functioning as a ligand binding module of FLIP. These FLIPs were successfully used for the determination of amino acid concentration in complex solutions as well as real-time measurement of amino acid influx in living yeast cells. Thus, the circular permutation strategy would not only improve the performance of each nanosensor but also expand the repertoire of metabolites that can be measured by the FLIP nanosensor technology. Published by Wiley-Blackwell.. |
| 20. | Satoshi Okada, Kazuhisa Ota, Takashi Ito, Circular permutation of ligand‐binding module improves dynamic range of genetically encoded FRET‐based nanosensor, Protein Science, 10.1002/pro.266, 18, 12, 2518-2527, 2009.12. |
| 21. | Kazuhisa Ota, Keiji Kito, Satoshi Okada, Takashi Ito, A proteomic screen reveals the mitochondrial outer membrane protein Mdm34p as an essential target of the F-box protein Mdm30p, Genes to Cells, 10.1111/j.1365-2443.2008.01228.x, 13, 10, 1075-1085, 2008.10, Ubiquitination plays various critical roles in eukaryotic cellular regulation and is medated by a cascade of enzymes including ubiquitin protein ligase (E3). The Skp1-Cullin-F-box protein complex comprises the largest E3 family, in each member of which a unique F-box protein binds its targets to define substrate specificity. Although genome sequencing uncovers a growing number of F-box proteins, most of them have remained as "orphans" because of the difficulties in identification of their substrates. To address this issue, we tested a quantitative proteomic approach by combining the stable isotope labeling by amino acids in cell culture (SILAC), parallel affinity purification (PAP) that we had developed for efficient enrichment of ubiquitinated proteins, and mass spectrometry (MS). We applied this SILAC-PAP-MS approach to compare ubiquitinated proteins between yeast cells with and without over-expressed Mdm30p, an F-box protein implicated in mitochondrial morphology. Consequently, we identified the mitochondrial outer membrane protein Mdm34p as a target of Mdm30p. Furthermore, we found that mitochondrial defects induced by deletion of MDM30 are not only recapitulated by a mutant Mdm34p defective in interaction with Mdm30p but alleviated by ubiquitination-mimicking forms of Mdm34p. These results indicate that Mdm34p is a physiologically important target of Mdm30p.. |
| 22. | Kazuhisa Ota, Keiji Kito, Satoshi Okada, Takashi Ito, A proteomic screen reveals the mitochondrial outer membrane protein Mdm34p as an essential target of the F‐box protein Mdm30p, Genes to Cells, 10.1111/j.1365-2443.2008.01228.x, 13, 10, 1075-1085, 2008.10. |
| 23. | Keiji Kito, Noriko Kawaguchi, Satoshi Okada, Takashi Ito, Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics, Proteomics, 10.1002/pmic.200800182, 8, 12, 2366-2370, 2008.06, To discriminate between stable and dynamic protein-protein interactions, we propose a strategy in which cells with and without tagged bait are differentially labeled with stable isotope and combined prior to complex purification. Mass-spectrometric analysis of the purified complexes identifies stable and dynamic components as those derived exclusively from the tagged cells and those from both cells, respectively. We successfully applied this strategy to analyze two yeast protein complexes, eIF2B-eIF2 and cyclin-Cdc28.. |
| 24. | Keiji Kito, Noriko Kawaguchi, Satoshi Okada, Takashi Ito, Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics, PROTEOMICS, 10.1002/pmic.200800182, 8, 12, 2366-2370, 2008.06, To discriminate between stable and dynamic protein-protein interactions, we propose a strategy in which cells with and without tagged bait are differentially labeled with stable isotope and combined prior to complex purification. Mass-spectrometric analysis of the purified complexes identifies stable and dynamic components as those derived exclusively from the tagged cells and those from both cells, respectively. We successfully applied this strategy to analyze two yeast protein complexes, eIF2B-eIF2 and cyclin-Cdc28.. |
| 25. | M Iwase, S Okada, T Oguchi, A Toh-e, Forchlorfenuron, a phenylurea cytokinin, disturbs septin organization in Saccharomyces cerevisiae, GENES & GENETIC SYSTEMS, 10.1266/ggs.79.199, 79, 4, 199-206, 2004.08, Septins, which are involved in cytokinesis, have been identified in a variety of fungi and animal cells. For analysis of the function of septin, drugs targeting septin would be useful; however, no such drugs have been available hitherto. By serendipity, we found that forchlorfenuron (FCF, N-(2-chloro-4-pyridyl)-N-phenylurea, 4PU300), a synthetic plant cytokinin, disturbed cytokinesis in Saccharomyces cerevisiae. Upon administration of FCF, septin structures at the bud neck became deformed and filament-like septin appeared outside of the neck. Under these conditions, the localization of actin was normal and Gin4, which is localized at the bud neck in a septin-dependent manner, was found to remain at the location of apparently normal septin at the bud neck, whereas it was not co-localized to the deformed septin at the bud neck or to septin seen outside the bud neck. FCF administration immediately induced production of sporadic septin structures outside the bud neck, and these structures disappeared promptly upon removal of the drug. Taken together, these findings indicate that FCF maybe a promising drug for investigating the structure and function of septin.. |
| 26. | Masayuki Iwase, Satoshi Okada, Tomoko Oguchi, Akio Toh-e, Forchlorfenuron, a phenylurea cytokinin, disturbs septin organization in Saccharomyces cerevisiae, Genes and Genetic Systems, 79, 4, 199-206, 2004.05, [URL]. |
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