Changes in sexual agglutination ability during the formation of vegetative cells from spores in Saccharomyces cerevisiae

1981 ◽  
Vol 183 (2) ◽  
pp. 205-208 ◽  
Author(s):  
Hiroshi Tohoyama ◽  
Naohiko Yanagishima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Vegetative Cells ◽  
Sexual Agglutination

scholarly journals A Role for MMS4 in the Processing of Recombination Intermediates During Meiosis in Saccharomyces cerevisiae

Genetics ◽  
2001 ◽  
Vol 159 (4) ◽  
pp. 1511-1525 ◽  
Author(s):  
Teresa de los Santos ◽  
Josef Loidl ◽  
Brittany Larkin ◽  
Nancy M Hollingsworth
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Meiotic Recombination ◽  
Biochemical Data ◽  
Dna Metabolism ◽  
Spore Viability ◽  
Vegetative Cells ◽  
Recombination Checkpoint

Abstract The MMS4 gene of Saccharomyces cerevisiae was originally identified due to its sensitivity to MMS in vegetative cells. Subsequent studies have confirmed a role for MMS4 in DNA metabolism of vegetative cells. In addition, mms4 diploids were observed to sporulate poorly. This work demonstrates that the mms4 sporulation defect is due to triggering of the meiotic recombination checkpoint. Genetic, physical, and cytological analyses suggest that MMS4 functions after the single end invasion step of meiotic recombination. In spo13 diploids, red1, but not mek1, is epistatic to mms4 for sporulation and spore viability, suggesting that MMS4 may be required only when homologs are capable of undergoing synapsis. MMS4 and MUS81 are in the same epistasis group for spore viability, consistent with biochemical data that show that the two proteins function in a complex. In contrast, MMS4 functions independently of MSH5 in the production of viable spores. We propose that MMS4 is required for the processing of specific recombination intermediates during meiosis.

Sexual Agglutination in Saccharomyces cerevisiae

Botanica Acta ◽  
1995 ◽  
Vol 108 (2) ◽  
pp. 63-66 ◽  
Author(s):  
Karin Hauser ◽  
W. Tanner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Sexual Agglutination

Translocation of zinc from vacuole to nucleus during yeast meiosis

1983 ◽  
Vol 25 (5) ◽  
pp. 415-419 ◽  
Author(s):  
Carl A. Bilinski ◽  
John J. Miller
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Staining Procedure ◽  
Vegetative Cells ◽  
Nuclear Compartments ◽  
Polyphosphate Bodies ◽  
Yeast Meiosis ◽  
Zinc Translocation

A novel staining procedure employing the UV fluorochrome DAPI (4′,6-diamidino-2-phenylindole∙2HCl) and dithizone (diphenylthiocarbazone) was developed for microcytochemical determination of sites of zinc localization in Saccharomyces cerevisiae Hansen. In vegetative cells vacuolar polyphosphate bodies stained with dithizone, whereas in sporulating cells nucleoli and centriolar plaques were dithizone-positive. Hence, dithizone not only permitted localization of zinc but also indicated zinc translocation from vacuolar to nuclear compartments during differentiation from the vegetative to sporulated state.

scholarly journals Inhibitory effects of nucleoside 5′-alkylphosphates on sexual agglutination in Saccharomyces cerevisiae

2006 ◽  
Vol 147 (1) ◽  
pp. 17-22
Author(s):  
Kiyotaka Machida ◽  
Toshio Tanaka ◽  
Kozo Shibata ◽  
Makoto Taniguchi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Inhibitory Effects ◽  
Sexual Agglutination

A SEROLOGICAL COMPARISON OF VEGETATIVE CELL AND ASCUS WALLS AND THE SPORE COAT OF SACCHAROMYCES CEREVISIAE

1966 ◽  
Vol 12 (3) ◽  
pp. 485-488 ◽  
Author(s):  
I. J. Snider ◽  
J. J. Miller
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Structure ◽  
Vegetative Cell ◽  
Proteolytic Enzyme ◽  
Spore Coat ◽  
Vegetative Cells

Cross-agglutination tests with sera obtained by injection of vegetative cells, asci, and spores into rabbits revealed no immunological distinction between the walls of vegetative cells and asci, whereas the spore coats were found to be serologically distinct from cell and ascus walls. Treatment of vegetative cells and asci with periodate or a proteolytic enzyme before agglutination tests gave results which suggest that the critical antigen is a protein structure.

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