scholarly journals The effects of sterol mutants of the yeast Saccharomyces cerevisiae on the outcome of competition between Drosophila melanogaster and D. simulans

Genetica ◽  
1983 ◽  
Vol 61 (2) ◽  
pp. 89-97
Author(s):  
M. Bos ◽  
A. Boerema ◽  
G. Lammers
1988 ◽  
Vol 8 (10) ◽  
pp. 4314-4321
Author(s):  
S J Brown ◽  
D D Rhoads ◽  
M J Stewart ◽  
B Van Slyke ◽  
I T Chen ◽  
...  

We describe a Drosophila DNA clone of tandemly duplicated genes encoding an amino acid sequence nearly identical to human ribosomal protein S14 and yeast rp59. Despite their remarkably similar exons, the locations and sizes of introns differ radically among the Drosophila, human, and yeast (Saccharomyces cerevisiae) ribosomal protein genes. Transcripts of both Drosophila RPS14 genes were detected in embryonic and adult tissues and are the same length as mammalian S14 message. Drosophila RPS14 was mapped to region 7C5-9 on the X chromosome. This interval also encodes a previously characterized Minute locus, M(1)7C.


1994 ◽  
Vol 14 (8) ◽  
pp. 5412-5424
Author(s):  
C J Yoo ◽  
S L Wolin

The human autoantigen La is a 50-kDa protein which binds to the 3' termini of virtually all nascent polymerase III transcripts. Experiments with mammalian transcription extracts have led to the proposal that the La protein is required for multiple rounds of transcription by RNA polymerase III (E. Gottlieb and J. A. Steitz, EMBO J. 8:851-861, 1989; R. J. Maraia, D. J. Kenan, and J. D. Keene, Mol. Cell. Biol. 14:2147-2158, 1994). Although La protein homologs have been identified in a variety of vertebrate species, the protein has not been identified in invertebrates. In order to begin a genetic analysis of La protein function, we have characterized homologs of the La protein in the fruit fly Drosophila melanogaster and the yeast Saccharomyces cerevisiae. We show that both the Drosophila and yeast La proteins are bound to precursors of polymerase III RNAs in vivo. The Drosophila and yeast proteins resemble the human La protein in their biochemical properties, as both proteins can be partially purified from cells by a procedure previously devised to purify the human protein. Similarly to vertebrate La proteins, the Drosophila and yeast homologs preferentially bind RNAs that terminate with a 3' hydroxyl. Despite the fact that the La protein is conserved between humans and Saccharomyces cerevisiae, yeast cells containing a null allele of the gene encoding the La protein are viable, suggesting that another protein(s) plays a functionally redundant role.


1988 ◽  
Vol 8 (10) ◽  
pp. 4314-4321 ◽  
Author(s):  
S J Brown ◽  
D D Rhoads ◽  
M J Stewart ◽  
B Van Slyke ◽  
I T Chen ◽  
...  

We describe a Drosophila DNA clone of tandemly duplicated genes encoding an amino acid sequence nearly identical to human ribosomal protein S14 and yeast rp59. Despite their remarkably similar exons, the locations and sizes of introns differ radically among the Drosophila, human, and yeast (Saccharomyces cerevisiae) ribosomal protein genes. Transcripts of both Drosophila RPS14 genes were detected in embryonic and adult tissues and are the same length as mammalian S14 message. Drosophila RPS14 was mapped to region 7C5-9 on the X chromosome. This interval also encodes a previously characterized Minute locus, M(1)7C.


1999 ◽  
Vol 34 (6) ◽  
pp. 399-404 ◽  
Author(s):  
Leo W. Parks ◽  
James H. Crowley ◽  
Frank W. Leak ◽  
Steven J. Smith ◽  
Michele E. Tomeo

1994 ◽  
Vol 14 (8) ◽  
pp. 5412-5424 ◽  
Author(s):  
C J Yoo ◽  
S L Wolin

The human autoantigen La is a 50-kDa protein which binds to the 3' termini of virtually all nascent polymerase III transcripts. Experiments with mammalian transcription extracts have led to the proposal that the La protein is required for multiple rounds of transcription by RNA polymerase III (E. Gottlieb and J. A. Steitz, EMBO J. 8:851-861, 1989; R. J. Maraia, D. J. Kenan, and J. D. Keene, Mol. Cell. Biol. 14:2147-2158, 1994). Although La protein homologs have been identified in a variety of vertebrate species, the protein has not been identified in invertebrates. In order to begin a genetic analysis of La protein function, we have characterized homologs of the La protein in the fruit fly Drosophila melanogaster and the yeast Saccharomyces cerevisiae. We show that both the Drosophila and yeast La proteins are bound to precursors of polymerase III RNAs in vivo. The Drosophila and yeast proteins resemble the human La protein in their biochemical properties, as both proteins can be partially purified from cells by a procedure previously devised to purify the human protein. Similarly to vertebrate La proteins, the Drosophila and yeast homologs preferentially bind RNAs that terminate with a 3' hydroxyl. Despite the fact that the La protein is conserved between humans and Saccharomyces cerevisiae, yeast cells containing a null allele of the gene encoding the La protein are viable, suggesting that another protein(s) plays a functionally redundant role.


2020 ◽  
pp. 257-262
Author(s):  
Leo W. Parks ◽  
James H. Crowley ◽  
Frank W. Leak ◽  
Steven J. Smith ◽  
Michele E. Tomeo

1976 ◽  
Vol 28 (2) ◽  
pp. 163-176 ◽  
Author(s):  
Marten Bos ◽  
Barrie Burnet ◽  
Roy Farrow ◽  
Robin A. Woods

SUMMARYFour species of Drosophila (melanogaster, simulans, mauritiana and virilis) were tested for their ability to survive on erg strains of Saccharomyces cerevisiae each having a mutant block at a different reaction in the synthesis of ergosterol. Species capable of completing development on a given yeast mutant strain were tested for egg production and viability, and also for their ability to survive on the mutant yeast for five complete generations. Sterol analyses using gas–liquid chromatography show that the sterol composition of flies closely resembles that of the yeasts on which they are grown, confirming that the steric criteria for sterols capable of a structural role in lipoprotein membranes are relatively broad. Even so, different sterols are not equally efficient in this respect and there are differences between species in their tolerance to the sterols available from each of the yeast mutants. The range of sterols capable of satisfying the micronutrient, as distinct from the macronutrient, requirement is narrower. Growth on two of the yeast mutants (erg-2 and erg-6) leads to developmental arrest in the larval stage due, it is suggested, to a block in the synthesis of ecdysone. The four Drosophila species lack an effective level of Δ8−Δ7 isomerase which is necessary for utilization of zymosterol and other Δ8 sterol precursors of ergosterol. Ergosta-5,7-diene-3β-ol appears to be capable of substituting for cholesterol in the metabolism of Drosophila.


2014 ◽  
Vol 50 (6) ◽  
pp. 569-576 ◽  
Author(s):  
A. M. Rumyantsev ◽  
G. A. Zakharov ◽  
A. V. Zhuravlev ◽  
M. V. Padkina ◽  
E. V. Savvateeva-Popova ◽  
...  

Genetics ◽  
1991 ◽  
Vol 127 (3) ◽  
pp. 475-488 ◽  
Author(s):  
V Guacci ◽  
D B Kaback

Abstract Distributive disjunction is defined as the first division meiotic segregation of either nonhomologous chromosomes that lack homologs or homologous chromosomes that have not recombined. To determine if chromosomes from the yeast Saccharomyces cerevisiae were capable of distributive disjunction, we constructed a strain that was monosomic for both chromosome I and chromosome III and analyzed the meiotic segregation of the two monosomic chromosomes. In addition, we bisected chromosome I into two functional chromosome fragments, constructed strains that were monosomic for both chromosome fragments and examined meiotic segregation of the chromosome fragments in the monosomic strains. The two nonhomologous chromosomes or chromosome fragments appeared to segregate from each other in approximately 90% of the asci analyzed, indicating that yeast chromosomes were capable of distributive disjunction. We also examined the ability of a small nonhomologous centromere containing plasmid to participate in distributive disjunction with the two nonhomologous monosomic chromosomes. The plasmid appeared to efficiently participate with the two full length chromosomes suggesting that distributive disjunction in yeast is not dependent on chromosome size. Thus, distributive disjunction in S. cerevisiae appears to be different from Drosophila melanogaster where a different sized chromosome is excluded from distributive disjunction when two similar size nonhomologous chromosomes are present.


1984 ◽  
Vol 4 (11) ◽  
pp. 963-972 ◽  
Author(s):  
Richard C. Nicholson ◽  
Larry A. Moran

A 3.52-kilobase (kb) segment of Drosophila melanogaster DNA carrying the 2.l5-kb transcribed sequence for the 70 000-dalton heat-shock protein hsp70) and l.l4-kb of the 5′ flanking sequence was inserted into an autonomously replicating chimeric plasmid and used to transform the yeast Saccharomyces cerevisiae. The Drosophila gene is efficiently transcribed in the transformed cells, yielding a transcript which is 21 nucleotides shorter than the normal Drosophila mRNA at the 5′ end. Significant increases in the amount of Drosophila-specific RNA occur when the transformed ceils are subjected to heat shock, indicating that the Drosophila gene is inducible in the yeast cells.


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