ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 11
    Electronic Resource
    Electronic Resource
    Dimerization of multiple maize ADHs studied in vivo and in vitro (1974)
    Springer
    Biochemical genetics 12 (1974), S. 407-417 
    Details
    ISSN: 1573-4927
    Keywords: maize ; alcohol dehydrogenase ; dissociation-reassociation ; dimerization ; gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Anaerobically induced primary roots simultaneously express two alcohol dehydrogenase (Adh) genes which specify three types of electrophoretically separable dimers: Set I, II, and III ADH. The S inbred line yields a particular activity ratio among these three sets. By use of an Adh 1 null mutant allele and in vitro chemical dissociation and reassociation of ADH dimers, these studies extrapolate from an ADH activity ratio to the actual ratio of ADH protein. Conclusions are that (1) ADH1 and ADH2 promoters dimerize randomly in vivo and in vitro, (2) the heterodimeric isozyme (Set II) is approximately the enzymological sum of its subunits under these assay conditions, and (3) ADH-2 subunits are from 10 to 20% as active as ADH1 subunits under these assay conditions. These conclusions imply that the unlinked Adh genes are coordinately regulated and reconfirm the two-gene-three-dimer model for the maize ADH isozymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486645
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 12
    Electronic Resource
    Electronic Resource
    Expression and distribution of cytosolic 6-phosphogluconate dehydrogenase isozymes in maize (1992)
    Springer
    Biochemical genetics 30 (1992), S. 233-246 
    Details
    ISSN: 1573-4927
    Keywords: phosphogluconate dehydrogenase ; isozymes ; maize ; gene dosage ; tissue-specific expression ; null alleles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Maize (Zea mays L.) cytosolic 6-phosphogluconate dehydrogenase isozymes (EC 1.1.1.44; 6-PGD) are encoded by unlinked lociPgd1 andPgd2. Two families from a Robertson's Mutator line were isolated which have no detectable expression ofPgd2. ThesePgd2-null mutants and aPgd1-null line were used to generate plants homozygous for null alleles at both cytosolic 6-PGD loci. The specific activity of 6-PGD in the double-null mutant was between 20 and 30% of wild-type levels in root extracts. The double-null mutant was reproductively viable in a moderate environment, suggesting that wild-type levels of cytosolic 6-PGD activity are not essential for growth. Isozyme dimer ratios in roots, leaves, and scutellum were binomial and reflected the wild-type gene copy number. 6-PGD isozymes showed tissue- and cell type-specific expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02396214
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 13
    Electronic Resource
    Electronic Resource
    Expression and distribution of cytosolic 6-phosphogluconate dehydrogenase isozymes in maize (1992)
    Springer
    Biochemical genetics 30 (1992), S. 233-246 
    Details
    ISSN: 1573-4927
    Keywords: phosphogluconate dehydrogenase ; isozymes ; maize ; gene dosage ; tissue-specific expression ; null alleles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Maize (Zea mays L.) cytosolic 6-phosphogluconate dehydrogenase isozymes (EC 1.1.1.44; 6-PGD) are encoded by unlinked lociPgd1 andPgd2. Two families from a Robertson's Mutator line were isolated which have no detectable expression ofPgd2. ThesePgd2-null mutants and aPgd1-null line were used to generate plants homozygous for null alleles at both cytosolic 6-PGD loci. The specific activity of 6-PGD in the double-null mutant was between 20 and 30% of wild-type levels in root extracts. The double-null mutant was reproductively viable in a moderate environment, suggesting that wild-type levels of cytosolic 6-PGD activity are not essential for growth. Isozyme dimer ratios in roots, leaves, and scutellum were binomial and reflected the wild-type gene copy number. 6-PGD isozymes showed tissue- and cell type-specific expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553752
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 14
    Electronic Resource
    Electronic Resource
    Genetic relationships between the multiple alcohol dehydrogenases of maize (1973)
    Springer
    Biochemical genetics 8 (1973), S. 27-36 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract There are three electrophoretically separable sets of alcohol dehydrogenase isozymes in maize. Previous work has shown that two of these isozymes (Sets I and II) share a subunit in common, since mutations in one of the Adh genes, Adh 1, alter both isozymes. A mutation in the second Adh gene, Adh 2, has now been induced and recovered. This mutant allele also alters two of the three isozymes—Sets III and II. Adh 1 and Adh 2 appear to segregate independently. Gel filtration data show that all ADH isozymes are indistinguishable in size. These findings support the hypothesis that the two Adh genes specify promoters which homo- and heterodimerize, yielding three types of ADH isozymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485554
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 15
    Electronic Resource
    Electronic Resource
    Simultaneous induction by anaerobiosis or 2,4-D of multiple enzymes specified by two unlinked genes: Differential Adh1-Adh2 expression in maize (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 215-227 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The data of this paper partially define a two-gene, differentially inducible enzyme system in maize. Four major conclusions are drawn. (1) Anaerobic treatment results in the simultaneous expression of two unlinked Adh genes, Adh1 and Adh2. Adh2 is scarcely expressed in the uninduced root and negligibly expressed in the quiescent embryo. (2) The zero-order rate of anaerobic ADH protein induction reflects the zero-order rate of ADH synthesis throughout the induction; all active ADH isozymes display negligible turnover during the induction. (3) The auxin, 2,4-D, overcomes “repression” by air. The aerobic induction rates are also zero-order with negligible turnover for any isozyme. (4) The ratio of Adh1-Adh2 expression is drastically altered dependent on the mode of induction. The level of this differential regulatory phenomenon is before or at the assembly of ADH polypeptides into enzymologically or antigenically active dimers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333761
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 16
    Electronic Resource
    Electronic Resource
    The Shrunken gene on chromosome 9 of Zea mays L is expressed in various plant tissues and encodes an anaerobic protein (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 461-468 
    Details
    ISSN: 1617-4623
    Keywords: Sucrose synthase ; Tissue-specific gene expression ; Anaerobic response ; Positive and negative control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Shrunken gene, located on the short arm of chromosome 9 of Zea mays, encodes the enzyme sucrose synthase (EC 2.4.1.13). The gene is known to be expressed in the endosperm of the developing maize kernel and seems to be involved in sucrose breakdown prior to starch synthesis. We have analyzed different tissues of the maize plant for transcripts of the Shrunken gene and have found rather high transcription rates in the etiolated shoot and the primary root of the germinating kernel. If the etiolated seedlings are illuminated, the transcript level drops by about 95% in the greening plant parts (1st and 2nd leaves) which are active in photosynthesis. A very low transcript level is found in mature green leaves where sucrose is formed from products of photosynthesis via a separate pathway. Upon anaerobic stress of the young seedling, the level of Shrunken transcripts increases 10 and 20 times in shoot and root tissue respectively. Apparently anaerobic induction supersedes the negative control that is observed after illumination in the 1st and 2nd leaves. From the experiments out-lined here we conclude that the anaerobic protein 87 (ANP87, Hake et al. 1985) is encoded by the Shrunken locus. While the expression of the Shrunken gene varies in different tissues and in response to external stimuli, transcription of the second sucrose synthase (B) gene seems to be irresponsive to anaerobic stress and to be expressed at a similar low level in all of the tissues examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00338083
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 17
    Electronic Resource
    Electronic Resource
    Selective synthesis of alcohol dehydrogenase during anaerobic treatment of maize (1978)
    Springer
    Molecular genetics and genomics 161 (1978), S. 111-115 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Anaerobic treatment of a maize seedling mediates the synthesis of five major, native proteins and seven polypeptide size-classes; slab polyacrylamide and autoradiographic techniques were used to analyze extracts from single primary roots. The alcohol dehydrogenase-1 polypeptide is most dramatically synthesized and accumulated during anaerobiosis, as compared to aerobic control data. Allozymes were used to identify alcohol dehydrogenase unequivocally. Our results pertain to interpretations of previous studies on the alcohol dehydrogenase gene system in maize, and to work on the stress proteins of Drosophila.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00274180
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 18
    Electronic Resource
    Electronic Resource
    Mutations of the Adh1 gene in maize following infection with barley stripe mosaic virus (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 367-369 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations at the Adh1 locus in maize were selected from plants infected with barley stripe mosaic virus (BSMV). Pollen from the infected inbred line 1s2p, which is homozygous for Adh1-S (abbreviated S), Adh2-P, c and r was treated with allyl alcohol and applied to silks of a tester stock homozygous for Adh1-F, Adh2-N, C and R. From these pollinations 356 kernels arose on the F1 ears. Of these eight showed no activity of the S allele in scutellar samples while two exhibited low levels. Five of the putative mutant kernels germinated and two of these contained the contamination markers Adh2-P, c and r. The newly arisen mutations were designated S5446 and S5453. S5453 exhibited an abnormally low level of ADH activity in the F1 scutellum. In the F2 generation the mutant reverted at a high frequency with only about 5% of the S5453 alleles expressing low levels. DNA blotting and hybridization analyses showed no alterations in the restriction patterns of S5453 when compared to the progenitor S allele. S5446 which exhibited no ADH activity in the F1 scutellum is unstable in the pollen; reversion frequencies approaching 10-2 were observed in samples from some plants. Restriction digestion patterns of DNA from this mutant revealed the presence of a 3.3 kb insertion at Adh. The insert does not appear to contain sequences homologous to the BSMV genome but rigorous analyses remain to be carried out. It is hypothesized that BSMV infection may mobilize endogenous but dormant transposable elements in maize.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332775
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 19
    Electronic Resource
    Electronic Resource
    Molecular analyses of genetically stable mutants of the maize Adh1 gene (1984)
    Springer
    Molecular genetics and genomics 194 (1984), S. 42-48 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 10 genetically stable mutants of the alcohol dehydrogenase-1 gene in maize were examined for ADH1-mRNA size and abundance, large changes in genomic restriction fragments, and intragenic recombination levels. Eight of the mutants were induced with ethyl methanesulfonate (EMS), four of which are CRM−; the other two mutants followed treatment with ionizing radiation. In general, EMS and ionizing radiation induce “point” lesions in Adh1 that, with few exceptions, do not alter the abundance or size of ADH1-RNA, or alter the gross genomic restriction map. One EMS mutant produced both normalsized and larger than normal ADH1-mRNA. The larger ADH1-mRNA appears to result from improper termination. Another mutant behaved as expected of an intragenic deletion in recombination tests but we found no abnormalities by restriction site mapping.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00383494
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 20
    Electronic Resource
    Electronic Resource
    Mutant alleles that are altered in quantitative, organ-specific behavior (1982)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 3 (1982), S. 179-196 
    Details
    ISSN: 0192-253X
    Keywords: alcohol dehydrogenase ; regulatory ; mutant ; mutable alleles ; organ-specific ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Three new mutant alleles of maize alcohol dehydrogenase-1 (Adh 1) were recovered following allyl alcohol selection of pollen. Each is altered in quantitative, organ-specific, regulatory properties. All mutant sites act in cis to the structural gene component. One mutant arose spontaneously, one followed indirectly from irradiation with high Z accelerated particles, and one was induced by an autonomous mutator system. Each mutant is assessed in three organs by utilizing ADH allozyme ratios that were quantified at the level of ADH enzyme activity and either [3H]-Leu incorporation into newly synthesized ADH 1 subunits or direct protein determinations. One mutation simultaneously raises Adh 1 expression in one organ and lowers it in another, another affects expression in one organ only, and another is extremely underexpressed in all organs but is unstable. This unstable allele has generated derivative mutant alleles that have less or zero ADH expression. We do not yet know whether or not coding sequences are involved in these mutants. We conclude that information for organ specificity and quantitative behavior resides near or within Adh 1 coding sequences.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020030302
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...