Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes

Ouellette, B. F. Francis; Mw, Clark; Keng, Teresa; Rk, Storms; Zhong, Wei; Zeng, Bin; Fortin, Natalie; Delaney, S. J.; Barton, Arnold B.; Db, Kaback

doi:10.1139/g93-005

Cited by 24 publications

(15 citation statements)

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“…Four microlitres of the 320-fold dilution were loaded. In the CYS3 promoter region, the sequence of this plasmid is identical to that published by Ono et al (1992) but differs by a 2 bp deletion from the sequence published by Ouellette et al (1993) at position -315 (our coordinates, see Figure 4).…”

Section: Dna Sequencingmentioning

confidence: 78%

The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae.

1995

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Initiation of meiotic recombination in the yeast Saccharomyces cerevisiae occurs by localized DNA double‐strand breaks (DSBs) at several locations in the genome, corresponding to hot spots for meiotic gene conversion and crossing over. The meiotic DSBs occur in regions of chromatin that are hypersensitive to nucleases. To gain insight into the molecular mechanism involved in the formation of these DSBs, we have determined their positions at the nucleotide level at the CYS3 hot spot of gene conversion on chromosome I. We found four major new features of these DSBs: (i) sites of DSBs are multiple with varying intensities and spacing within the promoter region of the CYS3 gene; (ii) no consensus sequence can be found at these sites, indicating that the activity involved in DSB formation has little or no sequence specificity; (iii) the breaks are generated by blunt cleavages; and (iv) the 5′ ends are modified in rad50S mutant strains, where the processing of these ends is known to be prevented. We present a model for the initiation of meiotic recombination taking into account the implications of these results.

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Section: Dna Sequencingmentioning

confidence: 78%

The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae.

1995

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“…8 (NCBI sequence ID 1419843)) lacks the four-cysteine [4Fe-4S] motif completely and presents an obvious exception to this consensus sequence. However, this sequence also encodes a putative mitochondrial leader sequence (28). Whether pairs of endonuclease III-like proteins, with and without [4Fe-4S] clusters, are present in other eukaryotic organisms and whether the non-Fe-S proteins are mitochondrial remains to be determined.…”

Section: Resultsmentioning

confidence: 99%

Cloning and Expression of the cDNA Encoding the Human Homologue of the DNA Repair Enzyme, Escherichia coli Endonuclease III

Hilbert

Chaung

Boorstein

et al. 1997

Journal of Biological Chemistry

142

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We previously purified a bovine pyrimidine hydratethymine glycol DNA glycosylase/AP lyase. The amino acid sequence of tryptic bovine peptides was homologous to Escherichia coli endonuclease III, theoretical proteins of Saccharomyces cerevisiae and Caenorhabditis elegans, and the translated sequences of rat and human 3 -expressed sequence tags (3 -ESTs) (Hilbert, T. P., Boorstein, R. J., Kung, H. C., Bolton, P. H., Xing, D., Cunningham, R. P., Teebor, G. W. (1996) Biochemistry 35, 2505-2511). Now the human 3 -EST was used to isolate the cDNA clone encoding the human enzyme, which, when expressed as a GST-fusion protein, demonstrated thymine glycol-DNA glycosylase activity and, after incubation with NaCNBH 3 , became irreversibly cross-linked to a thymine glycol-containing oligodeoxynucleotide, a reaction characteristic of DNA glycosylase/AP lyases. Amino acids within the active site, DNA binding domains, and [4Fe-4S] cluster of endonuclease III are conserved in the human enzyme. The gene for the human enzyme was localized to chromosome 16p13.2-.3. Genomic sequences encoding putative endonuclease III homologues are present in bacteria, archeons, and eukaryotes. The ubiquitous distribution of endonuclease III-like proteins suggests that the 5,6-double bond of pyrimidines is subject to oxidation, reduction, and/or hydration in the DNA of organisms of all biologic domains and that the resulting modified pyrimidines are deleterious to the organism.When a pyrimidine residue in cellular DNA becomes modified by oxidation, reduction, or hydration of its 5,6-double bond, repair is initiated by a DNA-glycosylase activity that cleaves the N-glycosyl bond of the damaged residue, releasing the modified base and creating an abasic (AP) site in the DNA backbone. Such DNA glycosylase activities have been identified in bacteria, yeast, and mammalian species (1-8) The first such enzyme described was Escherichia coli endonuclease III, which was identified not on the basis of its DNA glycosylase activity, but rather because it nicked UV-irradiated DNA (9). For this reason it was termed an endonuclease, because it was thought that nicking resulted from enzyme-catalyzed hydrolysis of internucleotide phosphodiester bonds at sites of DNA damage. It has since been determined that the enzyme nicks DNA not via hydrolysis, but by catalyzing ␤-elimination of the 3Ј-phosphate group at the AP site formed as a result of the enzyme's DNA glycosylase activity (10 -12). The modified base that was enzymatically released from UV-irradiated DNA proved to be cytosine and/or uracil hydrate (8). Enzymes that effect base release together with strand cleavage via ␤-elimination are now termed DNA glycosylase/AP lyases and, in addition to endonuclease III, include the Fpg protein of E. coli (13), the OGG1 protein of Saccharomyces cerevisiae (14, 15), and T4 endonuclease V (16).DNA glycosylase/AP lyases function through N-acylimine (Schiff's base) enzyme-substrate intermediates (17). Such enzyme-substrate intermediates can be chemically reduced to stable seco...

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“…4). Comparison of the putative amino acid sequence with sequences in the GenBank database indicated that MDMIO was previously identified as an open reading frame adjacent to the SP07 gene on chromosome I and was designated FUN37(FUN=funedon unknown now) (Whyte et al, 1990) and as YAL010 (Ouellette et al, 1993). The Mdml0p amino acid sequence does not display significant similarities to other known proteins, common motifs for functional sites, or characteristic targeting sequences for subcellular localization.…”

Section: Isolation and Analysis Of The Mdmio Genementioning

confidence: 99%

Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane.

Sogo

Yaffe

1994

The Journal of Cell Biology

269

232

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Abstract. Yeast cells with the mdm/0 mutation possess giant spherical mitochondria and are defective for mitochondrial inheritance. The giant mitochondria display classical features of mitochondrial ultrastructure, yet they appear incapable of movement or division. Genetic analysis indicated that the mutant phenotypes resulted from a single nuclear mutation, and the isolated MDMIO gene restored wild-type mitochondrial distribution and morphology when introduced into mutant cells. MDMIO encodes a protein of 56.2 kD located in the mitochondrial outer membrane. Depletion of Mdml0p from cells led to a condensation of normally extended, tubular mitochondria into giant spheres, and reexpression of the protein resulted in a rapid restoration of normal mitochondrial morphology. These results demonstrate that Mdml0p can control mitochondrial morphology, and that it plays a role in the inheritance of mitochondria. MITOCHONDRIAL inheritance is an essential component of cell proliferation (Yaffe, 1991b). This inheritance requires the growth and division of preexisting mitochondria and the distribution of mitochondria between daughter cells before cell division (Attardi and Schatz, 1988). Cytoskeletal elements have been implicated in the positioning and movement of mitochondria (Heggeness et al., 1978;Chen, 1988;McConnell and Yaffe, 1992;Drubin et al., 1993), but mechanisms underlying mitochondrial inheritance are poorly understood.Mitochondria are usually found as snakelike tubules, widely distributed in the eukaryotic cytoplasm (Tzagoloff, 1982;Bereiter-Hahn, 1990). Often, these tubules are interconnected into extended mitochondrial reticula (Stevens, 1981;Chen, 1988). Microscopic studies of live cells have revealed that these mitochondrial networks are extremely dynamic, with tubular processes undergoing frequent fragmentation, branching, and fusion, as well as redistribution within the cytoplasm (Bereiter-Hahn, 1990; Koning et ai., 1993). In addition to the dynamic properties of mitochondria found in most types of cells, certain pathological conditions lead to gross changes in mitochondrial morphology, including the development of giant mitochondria (Tandler and Hoppel, 1986;Inagaki et al., 1992). The molecular bases for these changes in mitochondrial morphology and distribution in both normal and diseased cells are unknown.We recently described several Saccharomyces cerevisiae mutants defective for mitochondrial inheritance (McConnell et al., 1990). These mitochondrial distribution and morphology (mdm) I mutants were identified by screening collections of temperature-sensitive strains by fluorescence microscopy for cells that failed to transfer mitochondria into daughter buds during incubation at the nonpermissive temperature. Analysis of two of these mutant strains led to the identification of a novel cytoskeletal component that mediates mitochondrial inheritance Yaffe, 1992, 1993), and it indicated a role for unsaturated fatty acids in mitochondrial movement (Stewart and Yaffe, 1991). Here, we describe a new mdm m...

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Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes

Cited by 24 publications

References 0 publications

The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae.

The nucleotide mapping of DNA double-strand breaks at the CYS3 initiation site of meiotic recombination in Saccharomyces cerevisiae.

Cloning and Expression of the cDNA Encoding the Human Homologue of the DNA Repair Enzyme, Escherichia coli Endonuclease III

Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane.

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