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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor (1989)
    [s.l.] : Nature Publishing Group
    Nature 337 (1989), S. 655-659 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Polyclonal antiserum raised against purified T. thermophila hsp60 (ref. 1) was used to isolate a segment of the yeast HSP60 gene by screening an expression library of genomic DNA fragments ligated into the A-phage vector Agtll (ref. 15). Analysis of a 3.0 kilobase (kb) yeast DNA fragment present in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/337655a0
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  • 2
    Electronic Resource
    Electronic Resource
    Mutations in a nuclear gene of Chlamydomonas cause the loss of two chloroplast ribosomal proteins, one synthesized in the chloroplast and the other in the cytoplasm (1984)
    Springer
    Current genetics 8 (1984), S. 369-378 
    Details
    ISSN: 1432-0983
    Keywords: Chlamydomonas ; Non-photosynthetic mutations ; Ribosome biogenesis ; Chloroplast ribosomal proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The allelic nuclear mutations of Chlamydomonas reinhardtii, cr-6 and cr-7, result in the loss of two proteins from the large subunit of the chloroplast ribosome. One of these proteins, L-13, is synthesized in the chloroplast and the other, L29, is made in the cytoplasm. The loss of these two proteins is correlated with the inability of the large subunits of the chloroplast ribosomes to form monomers which incorporate labeled phenylalanine at normal rates in response to a polyuridylic acid template. Using antisera raised against L13 and L29, we found that protein L-13 was synthesized in appreciable amounts in pulse labeled cells of cr-6 and cr-7, but protein L-29 was not. We conclude that the inability to synthesize protein L29 is a primary defect in both cr-6 and cr-7 and that this protein is required for the stable assembly of protein L-13 into chloroplast ribosomes. The absence of one or both of these proteins from the large subunit of chloroplast ribosomes of the mutants interferes with the ability of the small and large subunits to associate properly into normal 70S monomers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419826
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and characterization of MRP10, a yeast gene coding for a mitochondrial ribosomal protein (1997)
    Springer
    Current genetics 31 (1997), S. 228-234 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsSaccharomyces cerevisiae ; MRP10 ; Mitochondria ; Mitochondrial ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear gene MRP10 of Saccharomyces cerevisiae was cloned by complementation of a respiratory deficient mutant N518/L1. This mutant is defective in mitochondrial translation and shows a tendency to accumulate deletions in mitochondrial DNA (ρ –). Analysis revealed Mrp10p to be a component of the 37 S subunit of the mitochondrial ribosomes. Disruption of MRP10 in a haploid strain of yeast elicits a phenotype identical to that of the original mutant. The respiratory defect of the null mutant is rescued by re-introducing the MRP10 gene in a wild-type mitochondrial DNA background. These results indicate that Mrp10p belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation. Searches of current databases failed to reveal any homologs among known bacterial or eucaryotic cytoplasmic ribosomal proteins. Some sequence similarity, however, was detected between Mrp10p and Yml37p, previously identified as a component of the yeast mitochondrial 50 S ribosomal subunit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050199
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  • 4
    Electronic Resource
    Electronic Resource
    Candida albicans ALS3 and insights into the nature of the ALS gene family (1998)
    Springer
    Current genetics 33 (1998), S. 451-459 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsCandida albicans ; Gene family ; Hyphal-specific ; Differential gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ALS1 (agglutinin-like sequence) gene of Candida albicans encodes a protein similar to alpha-agglutinin, a cell-surface adhesion glycoprotein of Saccharomyces cerevisiae (Hoyer et al. 1995). A central domain of a tandemly repeated 108-bp sequence is found in the ALS1 coding region. This tandem-repeat motif hybridizes to multiple C. albicans genomic DNA fragments, indicating the possibility of other ALS1-like genes in C. albicans (Hoyer et al. 1995). To determine if these fragments constitute a gene family, tandem-repeat-hybridizing genomic fragments were isolated from a fosmid library by PCR screening using primers based on the consensus tandem-repeat sequence of ALS1 (Hoyer et al. 1995). One group of fosmids, designated ALS3, encodes a gene with 81% identity to ALS1. The sequences of ALS1 and ALS3 are most conserved in the tandem-repeat domain and in the region 5′ of the tandem repeats. Northern-blot analysis using unique probes from the 3′ end of each gene demonstrated that ALS1 expression varies, depending on which C. albicans strain is examined, and that ALS3 is hyphal-specific. Both genes are found in a variety of C. albicans and C. stellatoidea strains examined. The predicted Als1p and Als3p exhibit features suggesting that both are cell-surface glycoproteins. Southern blots probed with conserved sequences from the region 5′ of the tandem repeats suggest that other ALS-like sequences are present in the C. albicans genome and that the ALS family may be larger than originally estimated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050359
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  • 5
    Electronic Resource
    Electronic Resource
    Phenotypic analysis and molecular cloning of discolored-1 (dsc1), a maize gene required for early kernel development (1998)
    Springer
    Plant molecular biology 37 (1998), S. 483-493 
    Details
    ISSN: 1573-5028
    Keywords: maize ; transposon tagging ; embryo ; endosperm ; development ; dsc1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Recessive mutations in the maize dsc1 locus prevent normal kernel development. Solidification of the endosperm in homozygous dsc1− mutant kernels was undetectable 12 days after pollination, at which time the tissue was apparently completely solidified in wild-type kernels. At later times endosperm did solidify in homozygous dsc1− mutant kernels, but there was a marked reduction in the volume of the tissue. Embryo growth in homozygous dsc1− kernels was delayed compared to wild-type kernels, but proceeded to an apparently normal stage 1 in which the scutellum, coleoptile, and shoot apex were clearly defined. Embryo growth then ceased and the embryonic tissues degraded. Late in kernel development no tissue distinctions were obvious in dsc1− mutant embryos. Immature mutant embryos germinated when transplanted from kernels to tissue culture medium prior to embryonic degeneration, but only coleoptile proliferation was observed. The dsc1 gene was isolated by transposon tagging. Analysis of the two different dsc1− mutations confirmed that transposon insertion into the cloned genomic locus was responsible for the observed phenotype. Dsc1 mRNA was detected specifically in kernels 5–7 days after pollination. These data indicate Dsc1 function is required for progression of embryo development beyond a specific stage, and also is required for endosperm development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005998830723
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  • 6
    Electronic Resource
    Electronic Resource
    Recovery of mitochondrial DNA from blood leukocytes using detergent lysis (1992)
    Springer
    Biochemical genetics 30 (1992), S. 27-33 
    Details
    ISSN: 1573-4927
    Keywords: leukocytes ; DNA cloning ; mitochondrial DNA ; membrane solubilization ; subcellular fractionation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Mitochondrial DNA (mtDNA) was isolated from leukocytes contained in whole blood of cattle. Leukocyte membranes except the nuclear envelope were solubilized in a buffer that contained 1% Triton X-100. After sedimentation of cell nuclei, mtDNA was purified from the cell lysate by organic solvent extraction and ethanol precipitation. Approximately 5 µg of mtDNA was recovered from 400 ml of whole blood, a quantity sufficient for routine DNA cloning procedures or for detailed restriction mapping studies. mtDNA isolated with this method is a suitable substrate for several DNA-modifying enzymes. Thus, preparation of mtDNA from blood by detergent lysis provides a noninvasive alternative to tissue biopsy for characterization of mitochondrial genotypes in studies of evolutionary genetics and population dynamics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554425
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  • 7
    Electronic Resource
    Electronic Resource
    DNA sequence and transcript analysis of transposon MuA2, a regulator of Mutator transposable element activity in maize (1993)
    Springer
    Plant molecular biology 21 (1993), S. 1181-1185 
    Details
    ISSN: 1573-5028
    Keywords: Zea mays ; Mutator ; controlling element ; genomic DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 4942 bp DNA sequence of Zea mays transposon MuA2 was determined. Previous evidence indicated MuA2 controls activity of the Mu1 transposon located in the mutable allele a1-mum2. MuA2 contains two large, ATG-initiated open reading frames (ORFs) of 612 and 232 codons, respectively, located on opposite strands. MuA2 produces two transcripts, each containing one of these ORFs. Four different tandem direct repeat sequences are located downstream of the 612 codon ORF. The restriction map of MuA2 is identical to that of transposon MuR1, which also is known to regulate mutability of a1-mum2. Furthermore, except for a single nucleotide, MuA2 is identical to the Mutator element Mu9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00023614
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  • 8
    Electronic Resource
    Electronic Resource
    Yeast/E. coli shuttle vectors with multiple unique restriction sites (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 2 (1986), S. 163-167 
    Details
    ISSN: 0749-503X
    Keywords: Shuttle vectors ; gene cloning ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two yeast/E. coli shuttle vectors have been constructed. The two vectors, YEp351 and YEp352, have the following properties: (1) they can replicate autonomuosly in Saccharomyces cerevisiae and in E. coli; (2) they contain the β-lactamase gene and confer ampicillin resistance to E. coli; (3) they contain the entire sequence of pUC18; (4) all ten restriction sites of the multiple cloning region of pUC18 including EcoRI, SacI, KpnI, SmaI, BamH1, XbaI, SbaI, SalI, PstI, SphI and HindIII are unique in YEp352; these sites are also unique in YEp351 except for EcoRI and KpnI, which occur twice; (5) recombinant plasmids with DNA inserts in the multiple cloning region of YEp351 and YEp352 can be recognised by loss of β-galactosidase function in appropriate E. coli hosts; (6) YEp351 and YEp352 contain the yeast LEU2 and URA3 genes, respectively, allowing for selection of these grown under non-selective conditions indicative of high plasmid copy number. The above properties make the shuttle vectors suitable for constructions of yeast genomic libraries and for cloning of DNA fragments defined by a large number of different restriction sites.The two vectors have been further modified by deletion of the sequences necessary for antunomous replication in yeast. The derivative plasmids YIp651 and YIp352 can therefore be used ti integrate specific sequences into yeast chromosomal DNA.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320020304
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  • 9
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    Functions of maize genes encoding pyruvate phosphate dikinase in developing endosperm (2017)
    National Academy of Sciences
    Details
    Publication Date: 2017-12-18
    Description: Maize opaque2 (o2) mutations are beneficial for endosperm nutritional quality but cause negative pleiotropic effects for reasons that are not fully understood. Direct targets of the bZIP transcriptional regulator encoded by o2 include pdk1 and pdk2 that specify pyruvate phosphate dikinase (PPDK). This enzyme reversibly converts AMP, pyrophosphate, and phosphoenolpyruvate to ATP, orthophosphate, and pyruvate and provides diverse functions in plants. This study addressed PPDK function in maize starchy endosperm where it is highly abundant during grain fill. pdk1 and pdk2 were inactivated individually by transposon insertions, and both genes were simultaneously targeted by endosperm-specific RNAi. pdk2 accounts for the large majority of endosperm PPDK, whereas pdk1 specifies the abundant mesophyll form. The pdk1- mutation is seedling-lethal, indicating that C4 photosynthesis is essential in maize. RNAi expression in transgenic endosperm eliminated detectable PPDK protein and enzyme activity. Transgenic kernels weighed the same on average as nontransgenic siblings, with normal endosperm starch and total N contents, indicating that PPDK is not required for net storage compound synthesis. An opaque phenotype resulted from complete PPDK knockout, including loss of vitreous endosperm character similar to the phenotype conditioned by o2-. Concentrations of multiple glycolytic intermediates were elevated in transgenic endosperm, energy charge was altered, and starch granules were more numerous but smaller on average than normal. The data indicate that PPDK modulates endosperm metabolism, potentially through reversible adjustments to energy charge, and reveal that o2- mutations can affect the opaque phenotype through regulation of PPDK in addition to their previously demonstrated effects on storage protein gene expression.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Mechanistic Investigation of a Starch-Branching Enzyme Using Hydrodynamic Volume SEC Analysis (2008)
    American Chemical Society
    Details
    Publication Date: 2008-03-01
    Print ISSN: 1525-7797
    Electronic ISSN: 1526-4602
    Topics: Chemistry and Pharmacology
    Published by American Chemical Society
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