SPT10 and SPT21 are required for transcription of particular histone genes in Saccharomyces cerevisiae

The Saccharomyces cerevisiae genome contains four loci that encode histone proteins. Two of these loci, HTA1-HTB1 and HTA2-HTB2, each encode histones H2A and H2B. The other two loci, HHT1-HHF1 and HHT2-HHF2, each encode histones H3 and H4. Because of their redundancy, deletion of any one histone locus does not cause lethality. Previous experiments demonstrated that mutations at one histone locus, HTA1-HTB1, do cause lethality when in conjunction with mutations in the SPT10 gene. SPT10 has been shown to be required for normal levels of transcription of several genes in S. cerevisiae. Motivated by this double-mutant lethality, we have now investigated the interactions of mutations in SPT10 and in a functionally related gene, SPT21, with mutations at each of the four histone loci. These experiments have demonstrated that both SPT10 and SPT21 are required for transcription at two particular histone loci, HTA2-HTB2 and HHF2-HHT2, but not at the other two histone loci. These results suggest that under some conditions, S. cerevisiae may control the level of histone proteins by differential expression of its histone genes.

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SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes

Molecular and Cellular Biology ◽

10.1128/mcb.8.12.5132-5139.1988 ◽

1988 ◽

Vol 8 (12) ◽

pp. 5132-5139

Author(s):

D Thomas ◽

R Rothstein ◽

N Rosenberg ◽

Y Surdin-Kerjan

Keyword(s):

Saccharomyces Cerevisiae ◽

Gene Disruption ◽

Double Mutant ◽

State Level ◽

Functional Complementation ◽

The Other ◽

Steady State Level ◽

Duplicated Genes ◽

Double Mutant Strain ◽

Adomet Synthetase

In Saccharomyces cerevisiae the SAM1 and SAM2 genes encode two distinct forms of S-adenosylmethionine (AdoMet) synthetase. In a previous study we cloned and sequenced the SAM1 gene (D. Thomas and Y. Surdin-Kerjan, J. Biol. Chem. 262:16704-16709, 1987). In this work, the SAM2 gene was isolated by functional complementation of a yeast double-mutant strain, and its identity was ascertained by gene disruption. It has been sequenced and compared with the SAM1 gene. The degree of homology found between the two genes shows that SAM1 and SAM2 are duplicated genes. Using strains disrupted in one or the other SAM gene, we have studied the regulation of their expression by measuring the steady-state level of mRNA after growth under different conditions. The results show that the expression of the two SAM genes is regulated differently, SAM2 being induced by the presence of excess methionine in the growth medium and SAM1 being repressed under the same conditions. The level of mRNA in the parental strain shows that it is not the sum of the levels found in the two disrupted strains. This raises the question of how the two AdoMet synthetases in S. cerevisiae interact to control AdoMet synthesis.

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Two Novel Techniques for Determination of Polysaccharide Cross-Links Show that Crh1p and Crh2p Attach Chitin to both β(1-6)- and β(1-3)Glucan in the Saccharomyces cerevisiae Cell Wall

Eukaryotic Cell ◽

10.1128/ec.00228-09 ◽

2009 ◽

Vol 8 (11) ◽

pp. 1626-1636 ◽

Cited By ~ 49

Author(s):

Enrico Cabib

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Wall ◽

Acetic Acid ◽

Yeast Cell ◽

Cell Walls ◽

Double Mutant ◽

The Other ◽

Cross Links

ABSTRACT Previous work, using solubilization of yeast cell walls by carboxymethylation, before or after digestion with β(1-3)- or β(1-6)glucanase, followed by size chromatography, showed that the transglycosylases Crh1p and Crh2p/Utr2p were redundantly required for the attachment of chitin to β(1-6)glucan. With this technique, crh1Δ crh2Δ mutants still appeared to contain a substantial percentage of chitin linked to β(1-3)glucan. Two novel procedures have now been developed for the analysis of polysaccharide cross-links in the cell wall. One is based on the affinity of curdlan, a β(1-3)glucan, for β(1-3)glucan chains in carboxymethylated cell walls. The other consists of in situ deacetylation of cell wall chitin, generating chitosan, which can be extracted with acetic acid, either directly (free chitosan) or after digestion with different glucanases (bound chitosan). Both methodologies indicated that all of the chitin in crh1Δ crh2Δ strains is free. Reexamination of the previously used procedure revealed that the β(1-3)glucanase preparation used (zymolyase) is contaminated with a small amount of endochitinase, which caused erroneous results with the double mutant. After removing the chitinase from the zymolyase, all three procedures gave coincident results. Therefore, Crh1p and Crh2p catalyze the transfer of chitin to both β(1-3)- and β(1-6)glucan, and the biosynthetic mechanism for all chitin cross-links in the cell wall has been established.

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Spt10-Dependent Transcriptional Activation in Saccharomyces cerevisiae Requires both the Spt10 Acetyltransferase Domain and Spt21

Molecular and Cellular Biology ◽

10.1128/mcb.24.1.135-143.2004 ◽

2004 ◽

Vol 24 (1) ◽

pp. 135-143 ◽

Cited By ~ 27

Author(s):

David Hess ◽

Bingsheng Liu ◽

Nadia R. Roan ◽

Rolf Sternglanz ◽

Fred Winston

Keyword(s):

Saccharomyces Cerevisiae ◽

Transcriptional Activation ◽

Dependent Manner ◽

Histone Genes ◽

Key Factor ◽

A Cell ◽

Cycle Dependent ◽

Histone Locus ◽

Acetyltransferase Domain

ABSTRACT Histone levels are a key factor in several nuclear processes, including transcription and chromosome segregation. Previous studies have demonstrated that Spt10 and Spt21 are required for the normal transcription of a subset of the histone genes in Saccharomyces cerevisiae, and sequence analysis has suggested that Spt10 is an acetyltransferase. We have now characterized several aspects of transcriptional activation of histone genes by Spt10 in vivo. Our results show that activation by Spt10 is dependent on its acetyltransferase domain. At HTA2-HTB2, the histone locus whose transcription is most strongly dependent on Spt10, Spt10 is physically recruited to the promoter in an Spt21-dependent and a cell cycle-dependent manner. Furthermore, Spt10 and Spt21 directly interact. These results, taken together with the identification of spt10 mutations that suppress an spt21Δ mutation, suggest a model for transcriptional activation by Spt10 and Spt21.

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SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes.

Molecular and Cellular Biology ◽

10.1128/mcb.8.12.5132 ◽

1988 ◽

Vol 8 (12) ◽

pp. 5132-5139 ◽

Cited By ~ 89

Author(s):

D Thomas ◽

R Rothstein ◽

N Rosenberg ◽

Y Surdin-Kerjan

Keyword(s):

Saccharomyces Cerevisiae ◽

Gene Disruption ◽

Double Mutant ◽

State Level ◽

Functional Complementation ◽

The Other ◽

Steady State Level ◽

Duplicated Genes ◽

Double Mutant Strain ◽

Adomet Synthetase

In Saccharomyces cerevisiae the SAM1 and SAM2 genes encode two distinct forms of S-adenosylmethionine (AdoMet) synthetase. In a previous study we cloned and sequenced the SAM1 gene (D. Thomas and Y. Surdin-Kerjan, J. Biol. Chem. 262:16704-16709, 1987). In this work, the SAM2 gene was isolated by functional complementation of a yeast double-mutant strain, and its identity was ascertained by gene disruption. It has been sequenced and compared with the SAM1 gene. The degree of homology found between the two genes shows that SAM1 and SAM2 are duplicated genes. Using strains disrupted in one or the other SAM gene, we have studied the regulation of their expression by measuring the steady-state level of mRNA after growth under different conditions. The results show that the expression of the two SAM genes is regulated differently, SAM2 being induced by the presence of excess methionine in the growth medium and SAM1 being repressed under the same conditions. The level of mRNA in the parental strain shows that it is not the sum of the levels found in the two disrupted strains. This raises the question of how the two AdoMet synthetases in S. cerevisiae interact to control AdoMet synthesis.

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Faculty Opinions recommendation of Amplification of histone genes by circular chromosome formation in Saccharomyces cerevisiae.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1047068.498118 ◽

2006 ◽

Author(s):

Linda Breeden

Keyword(s):

Saccharomyces Cerevisiae ◽

Histone Genes ◽

Circular Chromosome ◽

Chromosome Formation

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Differential Expression of ATP Synthesis Related Gene in Fertility Conversion of Wheat BNS Male Sterile Line

ACTA AGRONOMICA SINICA ◽

10.3724/sp.j.1006.2014.01501 ◽

2014 ◽

Vol 40 (8) ◽

pp. 1501

Author(s):

Zhen WANG ◽

Xiao-Jing FAN ◽

Miao ZHANG ◽

Fang-Ning ZHANG ◽

Gui-Dong LI ◽

...

Keyword(s):

Differential Expression ◽

Atp Synthesis ◽

Related Gene ◽

Male Sterile ◽

Male Sterile Line

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Translation machinery reprogramming in programmed cell death in Saccharomyces cerevisiae

Cell Death Discovery ◽

10.1038/s41420-020-00392-x ◽

2021 ◽

Vol 7 (1) ◽

Author(s):

Francesco Monticolo ◽

Emanuela Palomba ◽

Maria Luisa Chiusano

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Death ◽

Acetic Acid ◽

Programmed Cell Death ◽

Differential Expression ◽

Ribosomal Proteins ◽

Relative Proportion ◽

Duplication Event ◽

Genome Duplication Event ◽

Cell Death Pathway

AbstractProgrammed cell death involves complex molecular pathways in both eukaryotes and prokaryotes. In Escherichia coli, the toxin–antitoxin system (TA-system) has been described as a programmed cell death pathway in which mRNA and ribosome organizations are modified, favoring the production of specific death-related proteins, but also of a minor portion of survival proteins, determining the destiny of the cell population. In the eukaryote Saccharomyces cerevisiae, the ribosome was shown to change its stoichiometry in terms of ribosomal protein content during stress response, affecting the relative proportion between ohnologs, i.e., the couple of paralogs derived by a whole genome duplication event. Here, we confirm the differential expression of ribosomal proteins in yeast also during programmed cell death induced by acetic acid, and we highlight that also in this case pairs of ohnologs are involved. We also show that there are different trends in cytosolic and mitochondrial ribosomal proteins gene expression during the process. Moreover, we show that the exposure to acetic acid induces the differential expression of further genes coding for products related to translation processes and to rRNA post-transcriptional maturation, involving mRNA decapping, affecting translation accuracy, and snoRNA synthesis. Our results suggest that the reprogramming of the overall translation apparatus, including the cytosolic ribosome reorganization, are relevant events in yeast programmed cell death induced by acetic acid.

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Recombination of Ty elements in yeast can be induced by a double-strand break.

Genetics ◽

10.1093/genetics/140.1.67 ◽

1995 ◽

Vol 140 (1) ◽

pp. 67-77 ◽

Cited By ~ 1

Author(s):

A Parket ◽

O Inbar ◽

M Kupiec

Keyword(s):

Saccharomyces Cerevisiae ◽

Cell Cycle ◽

Strand Break ◽

Double Strand Break ◽

The Other ◽

Direct Repeats ◽

Yeast Saccharomyces Cerevisiae ◽

Low Frequencies ◽

Ty Elements ◽

Main Family

Abstract The Ty retrotransposons are the main family of dispersed repeated sequences in the yeast Saccharomyces cerevisiae. These elements are flanked by a pair of long terminal direct repeats (LTRs). Previous experiments have shown that Ty elements recombine at low frequencies, despite the fact that they are present in 30 copies per genome. This frequency is not highly increased by treatments that cause DNA damage, such as UV irradiation. In this study, we show that it is possible to increase the recombination level of a genetically marked Ty by creating a double-strand break in it. This break is repaired by two competing mechanisms: one of them leaves a single LTR in place of the Ty, and the other is a gene conversion event in which the marked Ty is replaced by an ectopically located one. In a strain in which the marked Ty has only one LTR, the double-strand break is repaired by conversion. We have also measured the efficiency of repair and monitored the progression of the cells through the cell-cycle. We found that in the presence of a double-strand break in the marked Ty, a proportion of the cells is unable to resume growth.

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Influences of Histone Stoichiometry on the Target Site Preference of Retrotransposons Ty1 and Ty2 in Saccharomyces cerevisiae

Genetics ◽

10.1093/genetics/142.3.761 ◽

1996 ◽

Vol 142 (3) ◽

pp. 761-776 ◽

Cited By ~ 2

Author(s):

Lori A Rinckel ◽

David J Garfinkel

Keyword(s):

Saccharomyces Cerevisiae ◽

Promoter Region ◽

Target Site ◽

Site Preference ◽

Wild Type ◽

Histone Proteins ◽

Protein Levels ◽

In The Wild ◽

Type Strains ◽

Orientation Bias

Abstract In Saccharomyces cerevisiae, the target site specificity of the retrotransposon Ty1 appears to involve the Ty integration complex recognizing chromatin structures. To determine whether changes in chromatin structure affect Ty1 and Ty2 target site preference, we analyzed Ty transposition at the CAN1 locus in mutants containing altered levels of histone proteins. A Δhta1-htb1 mutant with decreased levels of H2A and H2B histone proteins showed a pattern of Ty1 and Ty2 insertions at CAN1 that was significantly different from that of both the wild-type and a Δhta2-htb2 mutant, which does not have altered histone protein levels. Altered levels of H2A and H2B proteins disrupted a dramatic orientation bias in the CAN1 promoter region. In the wild-type strains, few Ty1 and Ty2 insertions in the promoter region were oriented opposite to the direction of CAN1 transcription. In the Δhta1-htb1 background, however, numerous Ty1 and Ty2 insertions were in the opposite orientation clustered within the TATA region. This altered insertion pattern does not appear to be due to a bias caused by selecting canavanine resistant isolates in the different HTA1-HTB1 backgrounds. Our results suggest that reduced levels of histone proteins alter Ty target site preference and disrupt an asymmetric Ty insertion pattern.

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