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  • 1
    Online Resource
    Online Resource
    Sulfur Metabolism in Phototrophic Organisms. (2008)
    Dordrecht :Springer Netherlands,
    Details
    Keywords: Photosynthesis. ; Sulfur--Metabolism. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (538 pages)
    Edition: 1st ed.
    ISBN: 9781402068638
    Series Statement: Advances in Photosynthesis and Respiration Series ; v.27
    URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=372821
    DDC: 572.46
    Language: English
    Note: Hell_FM.pdf -- Hell_CP.pdf -- Hell_Ch01.pdf -- Hell_Ch02.pdf -- Hell_Ch03.pdf -- Hell_Ch04.pdf -- Hell_Ch05.pdf -- Hell_Ch06.pdf -- Hell_Ch07.pdf -- Hell_Ch08.pdf -- Hell_Ch09.pdf -- Hell_Ch10.pdf -- Hell_Ch11.pdf -- Hell_Ch12.pdf -- Hell_Ch13.pdf -- Hell_Ch14.pdf -- Hell_Ch15.pdf -- Hell_Ch16.pdf -- Hell_Ch17.pdf -- Hell_Ch18.pdf -- Hell_Ch19.pdf -- Hell_Ch20.pdf -- Hell_Ch21.pdf -- Hell_Ch22.pdf -- Hell_Ch23.pdf -- Hell_Ch24.pdf -- Hell_Index.pdf -- Hell_BM.pdf.
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  • 2
    Electronic Resource
    Electronic Resource
    PATHWAYS AND REGULATION OF SULFUR METABOLISM REVEALED THROUGH MOLECULAR AND GENETIC STUDIES (2000)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology and Plant Molecular Biology 51 (2000), S. 141-165 
    Details
    ISSN: 1040-2519
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Sulfur is essential for life. Its oxidation state is in constant flux as it circulates through the global sulfur cycle. Plants play a key role in the cycle since they are primary producers of organic sulfur compounds. They are able to couple photosynthesis to the reduction of sulfate, assimilation into cysteine, and further metabolism into methionine, glutathione, and many other compounds. The activity of the sulfur assimilation pathway responds dynamically to changes in sulfur supply and to environmental conditions that alter the need for reduced sulfur. Molecular genetic analysis has allowed many of the enzymes and regulatory mechanisms involved in the process to be defined. This review focuses on recent advances in the field of plant sulfur metabolism. It also emphasizes areas about which little is known, including transport and recycling/degradation of sulfur compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.arplant.51.1.141
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular genetics of sulfate assimilation in plants (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 97 (1996), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The sulfate assimilation pathway is the primary route by which higher plants obtain the sulfur necessary for growth. Sulfur is involved in a myriad of processes of central importance in metabolism. In the past few years much has been learned about this pathway and its regulation through analysis’of the genes encoding the enzymes and proteins that make up the sulfate assimilation pathway. The recent molecular genetic analysis builds on the biochemical and physiological groundwork of past studies. Further, gene analysis has provided the opportunity to compare directly the evolution of sulfate assimilation in plants and other organisms.,
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1996.970228.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    A new route for synthesis of dimethylsulphoniopropionate in marine algae (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 387 (1997), S. 891-894 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The 3-dimethylsulphoniopropionate (DMSP) produced by marine algae is the main biogenic precursor of atmospheric dimethylsulphide (DMS). This biogenic DMS, formed by bacterial and algal degradation of DMSP,, contributes about 1.5 × 1013 g of sulphur to the atmosphere ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/387891a0
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Evidence for the thiamine biosynthetic pathway in higher-plant plastids and its developmental regulation (1995)
    Springer
    Plant molecular biology 29 (1995), S. 809-821 
    Details
    ISSN: 1573-5028
    Keywords: Zea mays ; thiamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thiamine or vitamin B-1, is an essential constituent of all cells since it is a cofactor for two enzyme complexes involved in the citric acid cycle, pyruvate dehydrogenase and α-ketoglutarate dehydrogenase. Thiamine is synthesized by plants, but it is a dietary requirement for humans and other animals. The biosynthetic pathway for thiamine in plants has not been well characterized and none of the enzymes involved have been isolated. Here we report the cloning and characterization of two cDNAs representing members of the maize thi1 gene family encoding an enzyme of the thiamine biosynthetic pathway. This assignment was made based on sequence homology to a yeast thiamine biosynthetic gene and by functional complementation of a yeast strain in which the endogenous gene was inactivated. Using immunoblot analysis, the thi1 gene product was found to be located in a plastid membrane fraction. RNA gel blot analysis of various tissues and developmental stages indicated thi1 expression was differentially regulated in a manner consistent with what is known about thiamine synthesis in plants. This is the first report of cDNAs encoding proteins involved in thiamine biosynthesis for any plant species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00041170
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and analysis of the gene for cystathionine γ-synthase from Arabidopsis thaliana (1996)
    Springer
    Plant molecular biology 32 (1996), S. 1117-1124 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana cystathionine γ-synthase ; Escherichia coli ; functional complementation ; higher plants ; methionine biosynthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA clone, CGS1, encoding cystathionine γ-synthase (CGS) from Arabidopsis thaliana was selected by complementation of CGS mutant strain of Escherichia coli (metB). Cells expressing CGS1 can grow on medium lacking Met and contain CGS enzyme activity. Genomic DNA blot analysis of A. thaliana revealed that there is a single gene homologous with CGS1. A genomic fragment carrying CGS1 was cloned and sequenced. Through combined analysis of the cDNA and genomic clone it was determined that the CGS1 coding sequence is 1692 bp, encodes a 563 amino acid, 60 kDa protein, and is interrupted by ten introns. A transcriptional initiation site was detected 260 bp 5′ of the initiator codon. The predicted amino acid sequence of CGS1 contains a consensus pyridoxal phosphate-binding site and is similar to MetB of E. coli, with which it is 35 percent identical. The CGS1 product has a sequence at the amino terminus that resembles a transit peptide for localization to plastids. At least 160 amino acids from the amino terminus of the CGS1 enzyme are not essential for enzymatic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00041395
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of the isopentenyl diphosphate isomerase gene family from Arabidopsis thaliana (1998)
    Springer
    Plant molecular biology 36 (1998), S. 323-328 
    Details
    ISSN: 1573-5028
    Keywords: isoprenoid biosynthetic pathway ; functional complementation ; isopentenyl diphosphate isomerase ; higher plants ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two Arabidopsis thaliana cDNAs (IPP1 and IPP2) encoding isopentenyl diphosphate isomerase (IPP isomerase) were isolated by complementation of an IPP isomerase mutant strain of Saccharomyces cerevisiae. Both cDNAs encode enzymes with an amino terminus that may function as a transit peptide for localization in plastids. At least 31 amino acids from the amino terminus of the IPP1 protein and 56 amino acids from the amino terminus of the IPP2 protein are not essential for enzymatic activity. Genomic DNA blot analysis confirmed that IPP1 and IPP2 are derived from a small gene family in A. thaliana. Based on northern analysis expression of both cDNAs occurs predominantly in roots of mature A. thaliana plants grown to the pre-flowering stage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005935516274
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    Paper (German National Licenses)
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