A genetic analysis of glucoamylase activity in the diastatic yeast Saccharomyces cerevisiae NCYC 625

1990 ◽  
Vol 17 (4) ◽  
pp. 281-288 ◽  
Author(s):  
Daksha Patel ◽  
Ivor H. Evans ◽  
E. Alan Bevan
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Yeast Saccharomyces Cerevisiae ◽  
Glucoamylase Activity

scholarly journals DNA SEQUENCES OF FRAMESHIFT AND OTHER MUTATIONS INDUCED BY ICR-170 IN YEAST

Genetics ◽  
1985 ◽  
Vol 111 (2) ◽  
pp. 233-241
Author(s):  
Joachim F Ernst ◽  
D Michael Hampsey ◽  
Fred Sherman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Genetic Analysis ◽  
Dna Sequences ◽  
Induced Mutations ◽  
Sequence Analyses ◽  
Base Pairs ◽  
Yeast Saccharomyces Cerevisiae ◽  
Frameshift Mutations

ABSTRACT ICR-170-induced mutations in the CYC1 gene of the yeast Saccharomyces cerevisiae were investigated by genetic and DNA sequence analyses. Genetic analysis of 33 cyc1 mutations induced by ICR-170 and sequence analysis of eight representatives demonstrated that over one-third were frameshift mutations that occurred at one site corresponding to amino acid positions 29-30, whereas the remaining mutations were distributed more-or-less randomly, and a few of these were not frameshift mutations. The sequence results indicate that ICR-170 primarily induces G·C additions at sites containing monotonous runs of three G·C base pairs. However, some (see PDF) sites within the CYC1 gene were not mutated by ICR-170. Thus, ICR-170 is a relatively specific mutagen that preferentially acts on certain sites with monotonous runs of G·C base pairs.

scholarly journals Isolation and characterization of omnipotent suppressors in the yeast Saccharomyces cerevisiae.

Genetics ◽  
1990 ◽  
Vol 124 (3) ◽  
pp. 515-522
Author(s):  
L P Wakem ◽  
F Sherman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Low Temperatures ◽  
Carbon Sources ◽  
Yeast Saccharomyces Cerevisiae ◽  
Hypertonic Medium ◽  
Isolation And Characterization ◽  
Wide Range ◽  
Chromosome Ii

Abstract Approximately 290 omnipotent suppressors, which enhance translational misreading, were isolated in strains of the yeast Saccharomyces cerevisiae containing the psi+ extrachromosomal determinant. The suppressors could be assigned to 8 classes by their pattern of suppression of five nutritional markers. The suppressors were further distinguished by differences in growth on paromomycin medium, hypertonic medium, low temperatures (10 degrees), nonfermentable carbon sources, alpha-aminoadipic acid medium, and by their dominance and recessiveness. Genetic analysis of 12 representative suppressors resulted in the assignment of these suppressors to 6 different loci, including the three previously described loci SUP35 (chromosome IV), SUP45 (chromosome II) and SUP46 (chromosome II), as well as three new loci SUP42 (chromosome IV), SUP43 (chromosome XV) and SUP44 (chromosome VII). Suppressors belonging to the same locus had a wide range of different phenotypes. Differences between alleles of the same locus and similarities between alleles of different loci suggest that the omnipotent suppressors encode proteins that effect different functions and that altered forms of each of the proteins can effect the same function.

scholarly journals A CHROMOSOMAL TRANSLOCATION CAUSING OVERPRODUCTION OF ISO-2-CYTOCHROME c IN YEAST

Genetics ◽  
1978 ◽  
Vol 88 (4) ◽  
pp. 689-707 ◽  
Author(s):  
Fred Sherman ◽  
Cynthia Helms
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Genetic Analysis ◽  
Primary Structure ◽  
Reciprocal Translocation ◽  
Chromosomal Translocation ◽  
Normal Amount ◽  
Yeast Saccharomyces Cerevisiae ◽  
The Right ◽  
Structural Region

ABSTRACT The CYC7-1 mutation in the yeast Saccharomyces cerevisiae causes the production of approximately 30 times the normal amount of iso-2-cytochrome c. Genetic analysis established that the CYC7-1 mutation is a reciprocal translocation involving the left arm of chromosome V and the right arm of chromosome XVI. The chromosome V arm was broken adjacent to the gene CYC7, which determines the primary structure of iso-2-cytochrome c, and this fragment containing the CYC7 gene was joined to the segment of chromosome XVI. It appears as though the elevation of iso-2-cytochrome c is caused by an abnormal controlling region adjacent to the structural region of the CYC7 gene.

scholarly journals The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint

2002 ◽  
Vol 159 (5) ◽  
pp. 807-819 ◽  
Author(s):  
Tatiana Iouk ◽  
Oliver Kerscher ◽  
Robert J. Scott ◽  
Munira A. Basrai ◽  
Richard W. Wozniak
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Genetic Analysis ◽  
Nuclear Pore Complex ◽  
Spindle Assembly Checkpoint ◽  
Spindle Checkpoint ◽  
Spindle Assembly ◽  
Nuclear Pore ◽  
Yeast Saccharomyces Cerevisiae ◽  
Functional Link

Aphysical and functional link between the nuclear pore complex (NPC) and the spindle checkpoint machinery has been established in the yeast Saccharomyces cerevisiae. We show that two proteins required for the execution of the spindle checkpoint, Mad1p and Mad2p, reside predominantly at the NPC throughout the cell cycle. There they are associated with a subcomplex of nucleoporins containing Nup53p, Nup170p, and Nup157p. The association of the Mad1p–Mad2p complex with the NPC requires Mad1p and is mediated in part by Nup53p. On activation of the spindle checkpoint, we detect changes in the interactions between these proteins, including the release of Mad2p (but not Mad1p) from the NPC and the accumulation of Mad2p at kinetochores. Accompanying these events is the Nup53p-dependent hyperphosphorylation of Mad1p. On the basis of these results and genetic analysis of double mutants, we propose a model in which Mad1p bound to a Nup53p-containing complex sequesters Mad2p at the NPC until its release by activation of the spindle checkpoint. Furthermore, we show that the association of Mad1p with the NPC is not passive and that it plays a role in nuclear transport.

Genetic analysis of the Hsm3 protein domain structure in yeast Saccharomyces cerevisiae

2010 ◽  
Vol 46 (6) ◽  
pp. 652-658 ◽  
Author(s):  
A. Yu. Chernenkov ◽  
S. V. Ivanova ◽  
S. V. Kovaltzova ◽  
L. M. Gracheva ◽  
V. T. Peshekhonov ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Domain Structure ◽  
Protein Domain ◽  
Yeast Saccharomyces Cerevisiae ◽  
Protein Domain Structure

scholarly journals GAL4 protein: purification, association with GAL80 protein, and conserved domain structure.

1990 ◽  
Vol 10 (6) ◽  
pp. 2916-2923 ◽  
Author(s):  
D I Chasman ◽  
R D Kornberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Sequence Comparisons ◽  
Yeast Saccharomyces Cerevisiae ◽  
Conserved Domain ◽  
Antibody Sequence ◽  
Antipeptide Antibody ◽  
Carboxy Terminal ◽  
Plasmid Purification ◽  
High Copy Plasmid

Expression of the yeast Saccharomyces cerevisiae GAL4 protein under its own (galactose-inducible) control gave 5 to 10 times the level of protein observed when the GAL4 gene was on a high-copy plasmid. Purification of GAL4 by a procedure including affinity chromatography on a GAL4-binding DNA column yielded not only GAL4 but also a second protein, shown to be GAL80 by its reaction with an antipeptide antibody. Sequence comparisons of GAL4 and other members of a family of proteins sharing homologous cysteine finger motifs identified an additional region of homology in the middle of these proteins shown by genetic analysis to be important for GAL4 function. GAL4 could be cleaved proteolytically at the boundary of the conserved region, defining internal and carboxy-terminal folded domains.

GAL4 protein: purification, association with GAL80 protein, and conserved domain structure

1990 ◽  
Vol 10 (6) ◽  
pp. 2916-2923
Author(s):  
D I Chasman ◽  
R D Kornberg
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Genetic Analysis ◽  
Sequence Comparisons ◽  
Yeast Saccharomyces Cerevisiae ◽  
Conserved Domain ◽  
Antibody Sequence ◽  
Antipeptide Antibody ◽  
Carboxy Terminal ◽  
Plasmid Purification ◽  
High Copy Plasmid

Expression of the yeast Saccharomyces cerevisiae GAL4 protein under its own (galactose-inducible) control gave 5 to 10 times the level of protein observed when the GAL4 gene was on a high-copy plasmid. Purification of GAL4 by a procedure including affinity chromatography on a GAL4-binding DNA column yielded not only GAL4 but also a second protein, shown to be GAL80 by its reaction with an antipeptide antibody. Sequence comparisons of GAL4 and other members of a family of proteins sharing homologous cysteine finger motifs identified an additional region of homology in the middle of these proteins shown by genetic analysis to be important for GAL4 function. GAL4 could be cleaved proteolytically at the boundary of the conserved region, defining internal and carboxy-terminal folded domains.

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