Functional selection and analysis of yeast centromeric DNA

Hieter, Philip; Pridmore, David; Hegemann, Johannes H.; Thomas, Marjorie; Davis, Ronald W.; Philippsen, Peter

doi:10.1016/0092-8674(85)90287-9

Cited by 247 publications

(168 citation statements)

References 37 publications

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“…This result is similar to those for MET2 (3,29), MET3 (10) (43), and SAM] (56). Two identical sequence elements strongly resembling the UASMET consensus sequence TCACGTGA (28,54), which closely matches the RTCAC RTG CDE1 consensus sequence (19), are found in S. cerevisiae MET10 as CACGTGA (Fig. 3a, nt -232 to -226 and nt -250 to -244).…”

Section: Resultsmentioning

confidence: 99%

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

1994

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The yeast assimilatory sulfite reductase is a complex enzyme that is responsible for conversion of sulfite into sulfide. To obtain information on the nature of this enzyme, we In Saccharomyces cerevisiae, sulfate taken up from the surrounding environment is converted into sulfite through three enzymatic steps. Sulfite is further reduced to sulfide, which in turn combines with O-acetyl homoserine to form homocysteine and eventually methionine. A central step in this assimilation pathway is conversion of sulfite into sulfide, a six-electron transfer reaction catalyzed by the yeast assimilatory sulfite reductase (YSiR). YSiR was found to be NADPH dependent (35) and to contain the prosthetic groups flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), an iron-sulfur cluster and a nonflavin chromophore (61) later identified as siroheme (46), a uroporphyrinogen III derivative also found in bacterial sulfite reductases (33,34), and nitrite reductase (21). Some methionine auxotrophs of S. cerevisiae were found to possess a defective sulfite reductase devoid of FAD or of FAD and FMN (62). The mutants devoid only of FAD were later assigned to the metlO complementation group and shown to be affected solely in the sulfite reduction step (30,31). The results of Kobayashi and Yoshimoto (25) suggested that YSiR has an ct212 structure and that the molecular mass of

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Section: Resultsmentioning

confidence: 99%

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

1994

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“…The sequence which appeared bent by computer analysis but not by electrophoresis is found at position 500 bp in SV40 and is comprised of two bending elements. Because the elements are separated by 26 bp they cause bending in opposite directions, resulting in an "S" shaped computer modelled structure (data not shown). This structure would not be expected to exhibit marked electrophoretic retardation, in agreement with experimental results (8 and unpublished data).…”

Section: Resultsmentioning

confidence: 99%

“…The sequences of twelve of the sixteen i. cerevisiae CENs and two from the related yeast S. uvarum have been reported (23)(24)(25)(26)(27)(28)(29)(30). These sequences were studied by computer analysis.…”

Section: Resultsmentioning

confidence: 99%

Computer modelling of DNA structures involved in chromosome maintenance

Eckdahl

Anderson

1987

Nucl Acids Res

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Sequence-dependent DNA bending of synthetic and natural molecules was studied by computer analysis.Modelling of synthetic oligonucleotides and of 107 kb of natural sequences gave results which closely resembled published electrophoretic data, demonstrating the powerful predictive capacity of the procedure.The analysis was extended to the study of DNA structures involved in chromosome maintenance.Centromeric DNAs from yeast were found to have sequences in their functional elements which cause them to be unusually straight. Autonomous replicating sequences were found to have two structural domains, one consisting of unusually straight sequences surrounding the consensus and the other of bending elements in flanking DNA. In addition to a structural homology, centromeric and autonomous replicating sequences share common sequence elements.These observations show that computer modelling of natural sequences is a viable approach to the study of the biological implications of alternative DNA structures.

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“…Data bank search revealed, that the PRE3 gene is located 370 bp downstream of the CENlO nucleotide sequence [37] as shown in Fig. 1.…”

Section: Resultsmentioning

confidence: 99%

PRE3, highly homologous to the human major histocompatibility complex‐linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl‐peptide hydrolyzing activity

Enenkel¹,

Lehmann²,

Kipper³

et al. 1994

FEBS Letters

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20S proteasomes are multifunctional proteinase complexes ubiquitous in eucaryotes. We have cloned the yeast PRE3 gene by complementation of the pre3‐2 mutation, which leads to a defect in the peptidylglutamyl‐peptide hydrolyzing activity of the 20S proteasome. The PRE3 gene, a β‐type member of the proteasomal gene family, is essential for cellular life and codes for a 193‐amino acid proteasomal subunit with a predicted molecular mass of 21.2 kDa. The Pre3 protein shows striking homology to the human proteasome subunits Hsδ and Lmp2 (Ring12). Lmp2 is encoded in the major histocompatibility complex class II region implicating proteasomes in antigen processing.

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Functional selection and analysis of yeast centromeric DNA

Cited by 247 publications

References 37 publications

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

Two divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH

Computer modelling of DNA structures involved in chromosome maintenance

PRE3, highly homologous to the human major histocompatibility complex‐linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl‐peptide hydrolyzing activity

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