A calcineurin-like gene ppb1+ in fission yeast: mutant defects in cytokinesis, cell polarity, mating and spindle pole body positioning

1994 ◽  
Vol 107 (7) ◽  
pp. 1725-1735 ◽  
Author(s):  
T. Yoshida ◽  
T. Toda ◽  
M. Yanagida
Keyword(s):  
Cyclosporin A ◽  
Fission Yeast ◽  
Cell Polarity ◽  
Double Mutant ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Predicted Amino Acid Sequence ◽  
Null Mutant ◽  
Pole Body ◽  
Body Positioning

A calcineurin (type 2B)-like protein phosphatase gene designated ppb1+ was isolated from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequence was 57% identical to rat PP2B alpha. ppb1 null mutant could form colonies at 33 degrees C but the size of the colonies was small at 22 degrees C. Cytokinesis was greatly delayed at 22 degrees C, and a large number of multi-septate cells were produced. The cell polarity control was impaired, causing branched cells. ppb1 null was virtually sterile. These phenotypes were rescued by a plasmid carrying the ppb1+ gene. Multi-septate cells were also produced in wild type at 22 degrees C by cyclosporin A, an inhibitor of calcineurin. This drug effect was enhanced in stst1 null mutant, which was hypersensitive to various drugs and cations. ppb1 null was not affected by cyclosporin A, consistent with the hypothesis that ppb1 is its target. Double-mutant analysis indicated that ppb1 had a function related to that of two other phosphatases, type 1-like dis2 and 2A-like ppa2.ppb1 null-sts1 null showed the severe multi-septate phenotype in the absence of cyclosporin A. ppb1+ and sts1+ gene functions are related. The double mutant ppb1-sts5 was lethal, indicating that the ppb1+ gene shared an essential function with the sts5+ gene. Overexpression of ppb1+ caused anomalies in cell and nuclear shape, microtubule arrays and spindle pole body positioning in interphase cells. Thus the ppb1+ gene appears to be involved in cytokinesis, mating, transport, nuclear and spindle pole body positioning, and cell shape.

scholarly journals Cut1/separase C-terminus affects spindle pole body positioning in interphase of fission yeast: pointed nuclear formation

2002 ◽  
Vol 7 (11) ◽  
pp. 1113-1124 ◽  
Author(s):  
Takahiro Nakamura ◽  
Koji Nagao ◽  
Yukinobu Nakaseko ◽  
Mitsuhiro Yanagida
Keyword(s):  
Fission Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Pole Body ◽  
C Terminus ◽  
Body Positioning

scholarly journals Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation

2009 ◽  
Vol 187 (3) ◽  
pp. 413-427 ◽  
Author(s):  
Yuji Chikashige ◽  
Miho Yamane ◽  
Kasumi Okamasa ◽  
Chihiro Tsutsumi ◽  
Tomoko Kojidani ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Fission Yeast ◽  
Nuclear Membrane ◽  
Meiotic Prophase ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Null Mutant ◽  
Vegetative Cells ◽  
Nuclear Membranes ◽  
Pole Body

In many organisms, telomeres cluster to form a bouquet arrangement of chromosomes during meiotic prophase. Previously, we reported that two meiotic proteins, Bqt1 and -2, are required for tethering telomeres to the spindle pole body (SPB) during meiotic prophase in fission yeast. This study has further identified two novel, ubiquitously expressed inner nuclear membrane (INM) proteins, Bqt3 and -4, which are required for bouquet formation. We found that in the absence of Bqt4, telomeres failed to associate with the nuclear membranes in vegetative cells and consequently failed to cluster to the SPB in meiotic prophase. In the absence of Bqt3, Bqt4 protein was degraded during meiosis, leading to a phenotype similar to that of the bqt4-null mutant. Collectively, these results show that Bqt4 anchors telomeres to the INM and that Bqt3 protects Bqt4 from protein degradation. Interestingly, the functional integrity of telomeres is maintained even when they are separated from the nuclear envelope in vegetative cells.

Distinct nuclear and spindle pole body populations of cyclin–cdc2 in fission yeast

Nature ◽  
1990 ◽  
Vol 347 (6294) ◽  
pp. 680-682 ◽  
Author(s):  
Caroline E. Alfa ◽  
Bernard Ducommun ◽  
David Beach ◽  
Jeremy S. Hyams
Keyword(s):  
Fission Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Pole Body

scholarly journals Studies concerning the temporal and genetic control of cell polarity in Saccharomyces cerevisiae.

1991 ◽  
Vol 114 (3) ◽  
pp. 515-532 ◽  
Author(s):  
M Snyder ◽  
S Gehrung ◽  
B D Page
Keyword(s):  
Cell Cycle ◽  
Cell Polarity ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Yeast Cells ◽  
Cell Cycle Distribution ◽  
Restrictive Temperature ◽  
Microtubule Bundle ◽  
Pole Body ◽  
Capture Site

The establishment of cell polarity was examined in the budding yeast, S. cerevisiae. The distribution of a polarized protein, the SPA2 protein, was followed throughout the yeast cell cycle using synchronized cells and cdc mutants. The SPA2 protein localizes to a patch at the presumptive bud site of G1 cells. Later it concentrates at the bud tip in budded cells. At cytokinesis, the SPA2 protein is at the neck between the mother and daughter cells. Analysis of unbudded haploid cells has suggested a series of events that occurs during G1. The SPA2 patch is established very early in G1, while the spindle pole body residues on the distal side of the nucleus. Later, microtubules emanating from the spindle pole body intersect the SPA2 crescent, and the nucleus probably rotates towards the SPA2 patch. By middle G1, most cells contain the SPB on the side of the nucleus proximal to the SPA2 patch, and a long extranuclear microtubule bundle intersects this patch. We suggest that a microtubule capture site exists in the SPA2 staining region that stabilizes the long microtubule bundle; this capture site may be responsible for rotation of the nucleus. Cells containing a polarized distribution of the SPA2 protein also possess a polarized distribution of actin spots in the same region, although the actin staining is much more diffuse. Moreover, cdc4 mutants, which form multiple buds at the restrictive temperature, exhibit simultaneous staining of the SPA2 protein and actin spots in a subset of the bud tips. spa2 mutants contain a polarized distribution of actin spots, and act1-1 and act1-2 mutants often contain a polarized distribution of the SPA2 protein suggesting that the SPA2 protein is not required for localization of the actin spots and the actin spots are not required for localization of the SPA2 protein. cdc24 mutants, which fail to form buds at the restrictive temperature, fail to exhibit polarized localization of the SPA2 protein and actin spots, indicating that the CDC24 protein is directly or indirectly responsible for controlling the polarity of these proteins. Based on the cell cycle distribution of the SPA2 protein, a "cytokinesis tag" model is proposed to explain the mechanism of the non-random positioning of bud sites in haploid yeast cells.

scholarly journals The Fission Yeast Homolog of the Human Transcription Factor EAP30 Blocks Meiotic Spindle Pole Body Amplification

2005 ◽  
Vol 9 (1) ◽  
pp. 63-73 ◽  
Author(s):  
Ye Jin ◽  
Joel J. Mancuso ◽  
Satoru Uzawa ◽  
Daniela Cronembold ◽  
W. Zacheus Cande
Keyword(s):  
Transcription Factor ◽  
Fission Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Meiotic Spindle ◽  
Pole Body ◽  
Yeast Homolog ◽  
Human Transcription Factor

scholarly journals A microtubule polymerase cooperates with the kinesin-6 motor and a microtubule cross-linker to promote bipolar spindle assembly in the absence of kinesin-5 and kinesin-14 in fission yeast

2017 ◽  
Vol 28 (25) ◽  
pp. 3647-3659 ◽  
Author(s):  
Masashi Yukawa ◽  
Tomoki Kawakami ◽  
Masaki Okazaki ◽  
Kazunori Kume ◽  
Ngang Heok Tang ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Chromosome Segregation ◽  
Spindle Pole Body ◽  
Spindle Assembly ◽  
Spindle Pole ◽  
Temperature Sensitive ◽  
Bipolar Spindle ◽  
Pole Body ◽  
Cross Linker ◽  
Spindle Elongation

Accurate chromosome segregation relies on the bipolar mitotic spindle. In many eukaryotes, spindle formation is driven by the plus-end–directed motor kinesin-5 that generates outward force to establish spindle bipolarity. Its inhibition leads to the emergence of monopolar spindles with mitotic arrest. Intriguingly, simultaneous inactivation of the minus-end–directed motor kinesin-14 restores spindle bipolarity in many systems. Here we show that in fission yeast, three independent pathways contribute to spindle bipolarity in the absence of kinesin-5/Cut7 and kinesin-14/Pkl1. One is kinesin-6/Klp9 that engages with spindle elongation once short bipolar spindles assemble. Klp9 also ensures the medial positioning of anaphase spindles to prevent unequal chromosome segregation. Another is the Alp7/TACC-Alp14/TOG microtubule polymerase complex. Temperature-sensitive alp7cut7pkl1 mutants are arrested with either monopolar or very short spindles. Forced targeting of Alp14 to the spindle pole body is sufficient to render alp7cut7pkl1 triply deleted cells viable and promote spindle assembly, indicating that Alp14-mediated microtubule polymerization from the nuclear face of the spindle pole body could generate outward force in place of Cut7 during early mitosis. The third pathway involves the Ase1/PRC1 microtubule cross-linker that stabilizes antiparallel microtubules. Our study, therefore, unveils multifaceted interplay among kinesin-dependent and -independent pathways leading to mitotic bipolar spindle assembly.

Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast

2003 ◽  
Vol 270 (6) ◽  
pp. 449-461 ◽  
Author(s):  
F. Miki ◽  
A. Kurabayashi ◽  
Y. Tange ◽  
K. Okazaki ◽  
M. Shimanuki ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Hybrid Search ◽  
Pole Body ◽  
Membrane Bound ◽  
Two Hybrid

scholarly journals Spindle Pole Body Duplication in Fission Yeast Occurs at the G1/S Boundary but Maturation Is Blocked until Exit from S by an Event Downstream of Cdc10+

2004 ◽  
Vol 15 (12) ◽  
pp. 5219-5230 ◽  
Author(s):  
Satoru Uzawa ◽  
Fei Li ◽  
Ye Jin ◽  
Kent L. McDonald ◽  
Michael B. Braunfeld ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Spindle Pole Body ◽  
Specific Inhibitor ◽  
Spindle Pole ◽  
Feedback Mechanism ◽  
G1 Arrest ◽  
Restrictive Temperature ◽  
Permissive Temperature ◽  
Pole Body ◽  
In Cells

The regulation and timing of spindle pole body (SPB) duplication and maturation in fission yeast was examined by transmission electron microscopy. When cells are arrested at G1 by nitrogen starvation, the SPB is unduplicated. On release from G1, the SPBs were duplicated after 1–2 h. In cells arrested at S by hydroxyurea, SPBs are duplicated but not mature. In G1 arrest/release experiments with cdc2.33 cells at the restrictive temperature, SPBs remained single, whereas in cells at the permissive temperature, SPBs were duplicated. In cdc10 mutant cells, the SPBs seem not only to be duplicated but also to undergo partial maturation, including invagination of the nuclear envelope underneath the SPB. There may be an S-phase–specific inhibitor of SPB maturation whose expression is under control of cdc10+. This model was examined by induction of overreplication of the genome by overexpression of rum1p or cdc18p. In cdc18p-overexpressing cells, the SPBs are duplicated but not mature, suggesting that cdc18p is one component of this feedback mechanism. In contrast, cells overexpressing rum1p have large, deformed SPBs accompanied by other features of maturation and duplication. We propose a feedback mechanism for maturation of the SPB that is coupled with exit from S to trigger morphological changes.

scholarly journals Nuclear shape, growth and integrity in the closed mitosis of fission yeast depend on the Ran-GTPase system, the spindle pole body and the endoplasmic reticulum

2009 ◽  
Vol 122 (14) ◽  
pp. 2464-2472 ◽  
Author(s):  
Y. Gonzalez ◽  
K. Meerbrey ◽  
J. Chong ◽  
Y. Torii ◽  
N. N. Padte ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Fission Yeast ◽  
Spindle Pole Body ◽  
Spindle Pole ◽  
Nuclear Shape ◽  
Ran Gtpase ◽  
Pole Body
Sign in / Sign up

Export Citation Format

Share Document