scholarly journals Preliminary characterization of maturation-promoting factor from yeast Saccharomyces cerevisiae

1987 ◽  
Vol 88 (3) ◽  
pp. 273-281
Author(s):  
K. Tachibana ◽  
N. Yanagishima ◽  
T. Kishimoto
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Small Molecules ◽  
Sedimentation Coefficient ◽  
Restrictive Temperature ◽  
Dependent Manner ◽  
Yeast Saccharomyces Cerevisiae ◽  
Preliminary Characterization ◽  
M Phase ◽  
Maturation Promoting Factor

It has been known for some time that maturation-promoting factor (MPF) appears in a wide variety of eukaryotic cells at M phase and exerts equal M-phase-promoting activity in both meiotic cells and mitotic cells in a non-specific manner. MPF was extracted from cdc20 mutant cells of the yeast Saccharomyces cerevisiae synchronized at M phase by incubation at the restrictive temperature. When injected into immature oocytes of Xenopus laevis, yeast MPF caused meiosis reinitiation in a dose-dependent manner and even in the presence of cycloheximide. Yeast MPF exerted its activity in starfish oocytes as well. MPF activity was obtained only from cells in M phase and not from G1, S or G2 phase cells, indicating cyclical changes during the yeast mitotic cell cycle. Preliminary characterization of yeast MPF revealed that its activity was associated with a heat-labile protein having a sedimentation coefficient value of 6 S. In contrast to the current assumption that MPF is a Ca-sensitive phosphoprotein stabilized by phosphorylated small molecules, such as ATP and Na-beta-glycerophosphate, the present study revealed that yeast MPF was still active even after treatment with either Ca2+ or alkaline phosphatase. Furthermore, it was found that yeast MPF and these phosphorylated small molecules were complementary in inducing reinitiation of meiosis, since the meiosis-reinitiating activity was detected only when both were present simultaneously and almost undetectable when either of them was present alone.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Conservation of function and regulation within the Cdc28/cdc2 protein kinase family: characterization of the human Cdc2Hs protein kinase in Saccharomyces cerevisiae.

1989 ◽  
Vol 9 (9) ◽  
pp. 4064-4068 ◽  
Author(s):  
C Wittenberg ◽  
S I Reed
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Yeast Strain ◽  
Cell Cycle Progression ◽  
G1 Arrest ◽  
Yeast Saccharomyces Cerevisiae ◽  
Environmental Signals ◽  
Transgenic Yeast ◽  
M Phase

Whereas the Cdc28 protein kinase of the budding yeast Saccharomyces cerevisiae plays an essential role in cell cycle progression during the G1 interval, a function in the progression from the G2 interval into M phase has been inferred for its homologs, including the Cdc2Hs protein kinase of humans. To better understand these apparently disparate roles, we constructed a yeast strain in which the resident CDC28 gene was replaced by its human homolog, CDC2Hs. This transgenic yeast strain was able to perform the G1 functions attributed to the Cdc28 protein kinase, including the ability to grow and divide normally, to respond to environmental signals that induce G1 arrest, and to regulate the Cdc2Hs protein kinase appropriately in response to these signals.

Conservation of function and regulation within the Cdc28/cdc2 protein kinase family: characterization of the human Cdc2Hs protein kinase in Saccharomyces cerevisiae

1989 ◽  
Vol 9 (9) ◽  
pp. 4064-4068
Author(s):  
C Wittenberg ◽  
S I Reed
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Kinase ◽  
Yeast Strain ◽  
Cell Cycle Progression ◽  
G1 Arrest ◽  
Yeast Saccharomyces Cerevisiae ◽  
Environmental Signals ◽  
Transgenic Yeast ◽  
M Phase

Whereas the Cdc28 protein kinase of the budding yeast Saccharomyces cerevisiae plays an essential role in cell cycle progression during the G1 interval, a function in the progression from the G2 interval into M phase has been inferred for its homologs, including the Cdc2Hs protein kinase of humans. To better understand these apparently disparate roles, we constructed a yeast strain in which the resident CDC28 gene was replaced by its human homolog, CDC2Hs. This transgenic yeast strain was able to perform the G1 functions attributed to the Cdc28 protein kinase, including the ability to grow and divide normally, to respond to environmental signals that induce G1 arrest, and to regulate the Cdc2Hs protein kinase appropriately in response to these signals.

scholarly journals Cloning and characterization of four SIR genes of Saccharomyces cerevisiae.

1986 ◽  
Vol 6 (2) ◽  
pp. 688-702 ◽  
Author(s):  
J M Ivy ◽  
A J Klar ◽  
J B Hicks
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mating Type ◽  
Blot Analysis ◽  
Transcriptional Control ◽  
Genomic Library ◽  
Yeast Saccharomyces Cerevisiae ◽  
Mating Type Genes ◽  
Rna Blots

Mating type in the yeast Saccharomyces cerevisiae is determined by the MAT (a or alpha) locus. HML and HMR, which usually contain copies of alpha and a mating type information, respectively, serve as donors in mating type interconversion and are under negative transcriptional control. Four trans-acting SIR (silent information regulator) loci are required for repression of transcription. A defect in any SIR gene results in expression of both HML and HMR. The four SIR genes were isolated from a genomic library by complementation of sir mutations in vivo. DNA blot analysis suggests that the four SIR genes share no sequence homology. RNA blots indicate that SIR2, SIR3, and SIR4 each encode one transcript and that SIR1 encodes two transcripts. Null mutations, made by replacement of the normal genomic allele with deletion-insertion mutations created in the cloned SIR genes, have a Sir- phenotype and are viable. Using the cloned genes, we showed that SIR3 at a high copy number is able to suppress mutations of SIR4. RNA blot analysis suggests that this suppression is not due to transcriptional regulation of SIR3 by SIR4; nor does any SIR4 gene transcriptionally regulate another SIR gene. Interestingly, a truncated SIR4 gene disrupts regulation of the silent mating type loci. We propose that interaction of at least the SIR3 and SIR4 gene products is involved in regulation of the silent mating type genes.

scholarly journals The Highly Conserved tRNAHis Guanylyltransferase Thg1p Interacts with the Origin Recognition Complex and Is Required for the G2/M Phase Transition in the Yeast Saccharomyces cerevisiae

2005 ◽  
Vol 4 (4) ◽  
pp. 832-835 ◽  
Author(s):  
Terri S. Rice ◽  
Min Ding ◽  
David S. Pederson ◽  
Nicholas H. Heintz
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Origin Recognition Complex ◽  
Nuclear Division ◽  
Permissive Temperature ◽  
Yeast Saccharomyces Cerevisiae ◽  
M Phase ◽  
And Migration ◽  
Origin Recognition

ABSTRACT Here we show that the Saccharomyces cerevisiae tRNAHis guanylyltransferase Thg1p interacts with the origin recognition complex in vivo and in vitro and that overexpression of hemagglutinin-Thg1p selectively impedes growth of orc2-1(Ts) cells at the permissive temperature. Studies with conditional mutants indicate that Thg1p couples nuclear division and migration to cell budding and cytokinesis in yeast.

scholarly journals The Identification and Characterization of ADR6, a Gene Required for Sporulation and for Expression of the Alcohol Dehydrogenase II Isozyme From Saccharomyces cerevisiae

Genetics ◽  
1987 ◽  
Vol 116 (4) ◽  
pp. 523-530
Author(s):  
Aileen K W Taguchi ◽  
Elton T Young
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Isocitrate Lyase ◽  
Carbon Sources ◽  
Recessive Mutation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Upstream Activating Sequence ◽  
Adh Activity ◽  
Identification And Characterization

ABSTRACT The alcohol dehydrogenase II isozyme (enzyme, ADHII; structural gene, ADH2) of the yeast, Saccharomyces cerevisiae, is under stringent carbon catabolite control. This cytoplasmic isozyme exhibits negligible activity during growth in media containing fermentable carbon sources such as glucose and is maximal during growth on nonfermentable carbon sources. A recessive mutation, adr6-1, and possibly two other alleles at this locus, were selected for their ability to decrease Ty-activated ADH2-6 c expression. The adr6-1 mutation led to decreased ADHII activity in both ADH2-6c and ADH2+ strains, and to decreased levels of ADH2 mRNA. Ty transcription and the expression of two other carbon catabolite regulated enzymes, isocitrate lyase and malate dehydrogenase, were unaffected by the adr6-1 mutation. adr6-1/adr6-1strains were defective for sporulation, indicating that adr6 mutations may have pleiotropic effects. The sporulation defect was not a consequence of decreased ADH activity. Since the ADH2-6c mutation is due to insertion of a 5.6-kb Ty element at the TATAA box, it appears that the ADR6+-dependent ADHII activity required ADH2 sequences 3′ to or including the TATAA box. The ADH2 upstream activating sequence (UAS) was probably not required. The ADR6 locus was unlinked to the ADR1 gene which encodes another trans-acting element required for ADH2 expression.

A NON-NUCLEOTIDE POLYMER FOUND IN THE DNA OF THE SAND DOLLAR, ECHINARACHNIUS PARMA: II. PRELIMINARY CHARACTERIZATION

1967 ◽  
Vol 45 (2) ◽  
pp. 281-287 ◽  
Author(s):  
Herbert S. Rosenkranz
Keyword(s):  
Buoyant Density ◽  
Sedimentation Coefficient ◽  
Negative Electrode ◽  
Cesium Chloride ◽  
Amino Sugar ◽  
Electrophoretic Analysis ◽  
Positive Test ◽  
Preliminary Characterization ◽  
Acid Hydrolysate

A preliminary characterization of the non-nucleotidic component present in the DNA of Echinarachnius parma was undertaken. This material has an extremely high sedimentation coefficient (907 S). It contains no deoxyribose and presumably no ribose. After acid hydrolysis it was strongly ninhydrin-positive and also gave positive tests for reducing sugars as well as a slightly positive test for amino sugars. Upon electrophoretic analysis of an acid hydrolysate, three ninhydrinpositive spots were detected. One of these migrated to the negative electrode with a mobility identical with that of galactosamine, the other migrated to the positive electrode, and the third was neutral at pH 6.3. The spot with a mobility identical with that of galactosamine also gave a positive test for amino sugar. The material was not attacked by α-amylase. However, digestion with a crude trypsin preparation resulted in loss of the banding property in gradients of cesium chloride. Exposure to purified trypsin did not completely digest it, but caused an increase in buoyant density.

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