Cloning and analysis of the <i>Kluyveromyces lactis TRP1</i> gene: A chromosomal locus flanked by genes encoding inorganic pyrophosphatase and histone H3

Stark, Michael J. R.; Milner, J.

doi:10.1002/yea.320050106

Cited by 97 publications

(49 citation statements)

References 43 publications

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“…Chromosomal DNA was isolated and used in Southern-blot analysis, which revealed that a high percentage of the phleomycinresistant transformants contained the disruption fragment integrated at non-homologous positions in the genome (data not shown). This phenomenon of a high integration at non-homologous sites in K. lactis has also been observed by others (Stark and Milner 1989;Mulder et al 1994). Apparently, the process of homologous recombination in K. Iactis is less sequence-specific than it is in S. cerevisiae.…”

Section: The Kicpf1 Gene Is Essential For Cell Viability In K Laetissupporting

confidence: 80%

“…This yeast is related to S. cerevisiae and generally shows a high conservation of both sequence and function within structural genes (Stark and Milner 1989;Bergkamp-Steffens et al 1992), but tends to display an informative divergence of both features in regulatory factors, e.g., TFIIB (Na and Hampsey 1993), ABF1 (Gonqalves et al 1992), REB 1 (Morrow et al 1993) and HAP3 (Mulder et al 1994).…”

Section: Introductionmentioning

confidence: 99%

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Centromere promoter factors (CPF1) of the yeasts Saccharomyces cerevisiae and Kluyveromyces lactis are functionally exchangeable, despite low overall homology

Mulder¹,

Winkler

Scholten³

et al. 1994

Curr Genet

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General rightsIt is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. Download date: 10 May 2018Curr Genet (1994)26:198-207 Current Genetics The KICPF1 gene, coding for the centromere and promoter factor CPF1 from Kluyveromyces lactis, has been cloned by functional complementation of the methionine auxotrophic phenotype of a Saccharomyces cerevisiae mutant lacking ScCPF1. The amino-acid sequences of both CPF1 proteins show a relatively-low overall identity (31%), but a highly-homologous C-terminal domain (86%). This region constitutes the DNA-binding domain with basic-helix-loop-helix and leucine-zipper motifs, features common to the myc-related transcription factor family. The N-terminal two-thirds of the CPF1 proteins show no significant similarity, although the presence of acidic regions is a shared feature. In K1CPF1, the acidic region is a prominent stretch of approximately 40 consecutive aspartate and glutamate residues, suggesting that this part might be involved in transcriptional activation. In-vitro mobility-shift experiments were used to establish that both CPF1 proteins bind to the consensus binding site RTCACRTG (CDEI element). In contrast to S. cerevisiae, CPF1 genedisruption is lethal in K. lactis. The homologous CPF1 genes were transformed to both S. cerevisiae and K. lactis cpfl-null strains. Indistinguishable phenotypes were observed, indicating that, not withstanding the long nonconserved N-terminal region, the proteins are sufficiently homologous to overcome the phenotypes associated with cpfl gene-disruption.

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Section: The Kicpf1 Gene Is Essential For Cell Viability In K Laetissupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Centromere promoter factors (CPF1) of the yeasts Saccharomyces cerevisiae and Kluyveromyces lactis are functionally exchangeable, despite low overall homology

Mulder¹,

Winkler

Scholten³

et al. 1994

Curr Genet

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“…(A) Leftmap of VDE-reporter inserts at HIS4, showing digests used to detect recombination intermediates and products. One parent (P1) contains ARG4 sequences with a VDE-recognition site (arg4-VRS), flanked by an nourseothricin-resistance module [natMX, (Goldstein and McCusker, 1999)] and the Kluyveromyces lactis TRP1 gene [KlTRP1, (Stark and Milner, 1989)]; the other parent (P2) contains ARG4 sequences with a mutant, uncuttable VRS site [arg4-VRS103, (Nogami et al, 2002) flanked by URA3 and pBR322 sequences. Digestion with HindIII (H) and VDE (V) allows detection of crossovers (CO1 and CO2) and noncrossovers (NCO); digestion with HindIII alone allows detection of crossovers and DSBs.…”

Section: Resultsmentioning

confidence: 99%

Local chromosome context is a major determinant of crossover pathway biochemistry during budding yeast meiosis

Medhi¹,

Goldman

Lichten³

2016

Preprint

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The budding yeast genome contains regions where meiotic recombination initiates more frequently than in others. This pattern parallels enrichment for the meiotic chromosome axis proteins Hop1 and Red1. These proteins are important for Spo11-catalyzed double strand break formation; their contribution to crossover recombination remains undefined. Using the sequencespecific VMA1-derived endonuclease (VDE) to initiate recombination in meiosis, we show that chromosome structure influences the choice of proteins that resolve recombination intermediates to form crossovers. At a Hop1-enriched locus, most VDE-initiated crossovers, like most Spo11-initiated crossovers, required the meiosis-specific MutLg resolvase. In contrast, at a locus with lower Hop1 occupancy, most VDE-initiated crossovers were MutLg-independent. In pch2 mutants, the two loci displayed similar Hop1 occupancy levels, and VDE-induced crossovers were similarly MutLg-dependent. We suggest that meiotic and mitotic recombination pathways coexist within meiotic cells, and that features of meiotic chromosome structure determine whether one or the other predominates in different regions.

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“…Tyr 139, which forms a hydrogen bond to the anion in the present structure, can serve as a proton donor for this Pi. It is difficult to be certain Amino acid sequences have been determined for soluble PPases from Saccharomyces cerevisiae (cytoplasmic, Kolakowski et al, 1988; mitochondrial, Lundin et al, IWI), Schizosaccharomyces pombe (Kawasaki et al, 1990), Kluyveromyces lactis (Stark & Milner, 1989), bovine retina (Yang & Wensel, 1992), Arabidopsk thaliana (Kieber & Signer, 1991), E. coli (Lahti et al, 1988), Thermoplasma acidophilum (Richter & Schafer, 1992), thermophilic bacterium PS-3 (Ichiba et al, 1990), Bacillusstearothermophilus and 7: thermophilus (Ishii K, Shibuya K, Kaji H, Satoh T, Teplyakov A, Obmolova G , Kuranova I, Samejima T, manuscript in prep.). Their alignment clearly shows 2 distinct groups with much higher similarity inside the groups than between them.…”

Section: Active Center and Catalytic Mechanismmentioning

confidence: 99%

Crystal structure of inorganic pyrophosphatase from Thermus thermophilus

et al. 1994

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The 3-dimensional structure of inorganic pyrophosphatase from Therrnus thermophilus (T-PPase) has been determined by X-ray diffraction at 2.0 A resolution and refined to R = 15.3%. The structure consists of an antiparallel closed @sheet and 2 a-helices and resembles that of the yeast enzyme in spite of the large difference in size (174 and 286 residues, respectively), little sequence similarity beyond the active center (about 20%), and different oligomeric organization (hexameric and dimeric, respectively). The similarity of the polypeptide folding in the 2 PPases provides a very strong argument in favor of an evolutionary relationship between the yeast and bacterial enzymes. The same Greek-key topology of the 5-stranded 0-barrel was found in the OB-fold proteins, the bacteriophage gene-5 DNA-binding protein, toxic-shock syndrome toxin-1, and the major cold-shock protein of Bacillus subtilis. Moreover, all known nucleotide-binding sites in these proteins are located on the same side of the 0-barrel as the active center in T-PPase. Analysis of the active center of T-PPase revealed 17 residues of potential functional importance, 16 of which are strictly conserved in all sequences of soluble PPases. Their possible role in the catalytic mechanism is discussed on the basis of the present crystal structure and with respect to site-directed mutagenesis studies on the Escherichia coli enzyme. The observed oligomeric organization of T-PPase allows us to suggest a possible mechanism for the allosteric regulation of hexameric PPases.

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Cloning and analysis of the Kluyveromyces lactis TRP1 gene: A chromosomal locus flanked by genes encoding inorganic pyrophosphatase and histone H3

Cited by 97 publications

References 43 publications

Centromere promoter factors (CPF1) of the yeasts Saccharomyces cerevisiae and Kluyveromyces lactis are functionally exchangeable, despite low overall homology

Centromere promoter factors (CPF1) of the yeasts Saccharomyces cerevisiae and Kluyveromyces lactis are functionally exchangeable, despite low overall homology

Local chromosome context is a major determinant of crossover pathway biochemistry during budding yeast meiosis

Crystal structure of inorganic pyrophosphatase from Thermus thermophilus

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