scholarly journals Parametric analysis of length distributions of the fission yeast, Schizosaccharomyces pombe, in chemostat culture.

1995 ◽  
Vol 41 (1) ◽  
pp. 63-73 ◽  
Author(s):  
HISAO MIYATA ◽  
MACHIKO MIYATA ◽  
BYRON F. JOHNSON
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Parametric Analysis ◽  
Chemostat Culture

Patterns of extension growth of the fission yeast, Schizosaccharomyces pombe

1986 ◽  
Vol 32 (6) ◽  
pp. 528-530 ◽  
Author(s):  
H. Miyata ◽  
M. Miyata ◽  
Byron F. Johnson
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Dilution Rate ◽  
Progenitor Cells ◽  
Progenitor Cell ◽  
Chemostat Culture ◽  
Time Lapse ◽  
Extension Growth ◽  
Previous Cycle ◽  
Time Lapse Photomicrography

The growth of sausage-shaped cells of the fission yeast, Schizosaccharomyces pombe (strain NCYC 132), was followed in the second or third cycle by time-lapse photomicrography. Experimental cells were harvested from glucose-limited (0.2% glucose EMM3) chemostat culture (dilution rate, 0.125/h) and were plated onto a slide with EMM3 agar (2% glucose). By observing their extension patterns, we found some rules of extension growth. Thus, (1) all sibs with walls newly formed in the previous cycle, whose progenitor cells grew at the old end (followed Mitchison's rule), grow at the old end (also follow Mitchison's rule). (2) Sibs with old walls whose progenitor cell followed Mitchison's rule behave in one of three ways: (i) growth at the old end (follow Mitchison's rule); (ii) growth at the new end (violate Mitchison's rule); or (iii) growth at both ends (bipolar). (3) Both sibs whose progenitor grew at both ends (bipolar) always grow at the old end (follow Mitchison's rule).

scholarly journals Upstream – News in Genomics

2002 ◽  
Vol 3 (3) ◽  
pp. 221-225
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ovarian Cancer ◽  
Oryza Sativa ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Proteomic Analysis ◽  
Large Scale ◽  
Protein Complexes ◽  
The Other ◽  
Blood Samples

In recent months a bumper crop of genomes has been completed, including the fission yeast (Schizosaccharomyces pombe) and rice (Oryza sativa). Two large-scale studies ofSaccharomyces cerevisiaeprotein complexes provided a picture of the eukaryotic proteome as a network of complexes. Amongst the other stories of interest was a demonstration that proteomic analysis of blood samples can be used to detect ovarian cancer, perhaps even as early as stage I.

scholarly journals Analysis of centromeric DNA in the fission yeast Schizosaccharomyces pombe.

1986 ◽  
Vol 83 (21) ◽  
pp. 8253-8257 ◽  
Author(s):  
L. Clarke ◽  
H. Amstutz ◽  
B. Fishel ◽  
J. Carbon
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Centromeric Dna

Transport of l-lysine in the fission yeast Schizosaccharomyces pombe

1989 ◽  
Vol 978 (2) ◽  
pp. 203-208 ◽  
Author(s):  
Hana Sychrová ◽  
Jaroslav Horák ◽  
Arnošt Kotyk
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast

scholarly journals Assembly of normal actomyosin rings in the absence of Mid1p and cortical nodes in fission yeast

2008 ◽  
Vol 183 (6) ◽  
pp. 979-988 ◽  
Author(s):  
Yinyi Huang ◽  
Hongyan Yan ◽  
Mohan K. Balasubramanian
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Ring Structure ◽  
Contractile Ring ◽  
Ring Assembly ◽  
Cell Biol ◽  
In Cells

Cytokinesis in many eukaryotes depends on the function of an actomyosin contractile ring. The mechanisms regulating assembly and positioning of this ring are not fully understood. The fission yeast Schizosaccharomyces pombe divides using an actomyosin ring and is an attractive organism for the study of cytokinesis. Recent studies in S. pombe (Wu, J.Q., V. Sirotkin, D.R. Kovar, M. Lord, C.C. Beltzner, J.R. Kuhn, and T.D. Pollard. 2006. J. Cell Biol. 174:391–402; Vavylonis, D., J.Q. Wu, S. Hao, B. O'Shaughnessy, and T.D. Pollard. 2008. Science. 319:97–100) have suggested that the assembly of the actomyosin ring is initiated from a series of cortical nodes containing several components of this ring. These studies have proposed that actomyosin interactions bring together the cortical nodes to form a compacted ring structure. In this study, we test this model in cells that are unable to assemble cortical nodes. Although the cortical nodes play a role in the timing of ring assembly, we find that they are dispensable for the assembly of orthogonal actomyosin rings. Thus, a mechanism that is independent of cortical nodes is sufficient for the assembly of normal actomyosin rings.

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