Regulation of the production of the agglutination substances responsible for sexual agglutination in Saccharomyces cerevisiae: Changes associated with conjugation and temperature shift

1979 ◽  
Vol 174 (3) ◽  
pp. 269-280 ◽  
Author(s):  
Hiroshi Tohoyama ◽  
Michio Hagiya ◽  
Kazuo Yoshida ◽  
Naohike Yanagishina
1983 ◽  
Vol 3 (3) ◽  
pp. 457-465
Author(s):  
C H Kim ◽  
J R Warner

In Saccharomyces cerevisiae the synthesis of ribosomal proteins declines temporarily after a culture has been subjected to a mild temperature shock, i.e., a shift from 23 to 36 degrees C, each of which support growth. Using cloned genes for several S. cerevisiae ribosomal proteins, we found that the changes in the synthesis of ribosomal proteins parallel the changes in the concentration of mRNA of each. The disappearance and reappearance of the mRNA is due to a brief but severe inhibition of the transcription of each of the ribosomal protein genes, although the total transcription of mRNA in the cells is relatively unaffected by the temperature shock. The precisely coordinated response of these genes, which are scattered throughout the genome, suggests that either they or the enzyme which transcribes them has unique properties. In certain S. cerevisiae mutants, the synthesis of ribosomal proteins never recovers from a temperature shift. Yet both the decline and the resumption of transcription of these genes during the 30 min after the temperature shift are indistinguishable from those in wild-type cells. The failure of the mutant cells to grow at the restrictive temperature appears to be due to their inability to process the RNA transcribed from genes which have introns (Rosbash et al., Cell 24:679-686, 1981), a large proportion of which appear to be ribosomal protein genes.


1987 ◽  
Vol 7 (1) ◽  
pp. 244-250
Author(s):  
D Y Shin ◽  
K Matsumoto ◽  
H Iida ◽  
I Uno ◽  
T Ishikawa

When Saccharomyces cerevisiae cells grown at 23 degrees C were transferred to 36 degrees C, they initiated synthesis of heat shock proteins, acquired thermotolerance to a lethal heat treatment given after the temperature shift, and arrested their growth transiently at the G1 phase of the cell division cycle. The bcy1 mutant which resulted in production of cyclic AMP (cAMP)-independent protein kinase did not synthesize the three heat shock proteins hsp72A, hsp72B, and hsp41 after the temperature shift. The bcy1 cells failed to acquire thermotolerance to the lethal heat treatment and were not arrested at the G1 phase after the temperature shift. In contrast, the cyr1-2 mutant, which produced a low level of cAMP, constitutively produced three heat shock proteins and four other proteins without the temperature shift and was resistant to the lethal heat treatment. The results suggest that a decrease in the level of cAMP-dependent protein phosphorylation results in the heat shock response, including elevated synthesis of three heat shock proteins, acquisition of thermotolerance, and transient arrest of the cell cycle.


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

2006 ◽  
Vol 147 (1) ◽  
pp. 17-22
Author(s):  
Kiyotaka Machida ◽  
Toshio Tanaka ◽  
Kozo Shibata ◽  
Makoto Taniguchi

1981 ◽  
Vol 148 (3) ◽  
pp. 889-896 ◽  
Author(s):  
K Terrance ◽  
P N Lipke

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