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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Company
    Nature biotechnology 8 (1990), S. 768-768 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] To the editor: In response to the article by Pamela Knight entitled “Nucleic Acid and Protein Blotting,” (Bio/Technology 8:465, May '90) we would like to point out that there is no real “crosslinking controversy.” The vast majority of researchers have successfully used in ...
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  • 2
    ISSN: 1432-2048
    Keywords: Flower induction ; Flowering ; Nicotiana (flowering) ; Root and flowering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The interaction between roots and leaves as a function of the capacity of differently positioned leaves to induce flowering of four cultivars of Nicotiana tabacum L. was assessed under long-and short-day growth conditions with three types of manipulations: 1) repeated rooting of the shoot tip, 2) removal of apical leaves, and 3) removal of basal leaves. Repeated rooting of the shoot tip increased the number of nodes produced by all cultivars; however, a substantial extension of vegetative growth was only caused by rerooting in conditions where apical leaves exhibited little or no inductive capacity. The simplest and most consistent interpretation of these data is that floral initiation in tobacco results from an interaction of inputs from the leaves and the roots and that the root influence can be overridden by a strong leaf signal.
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  • 3
    ISSN: 1432-2048
    Keywords: Flowering ; Nicotiana (floral determination) ; Terminal bud ; Short-day plant ; Photoperiodism (flowering)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Floral determination in the terminal bud of the short-day plant Nicotiana tabacum cv. Maryland Mammoth has been investigated. Plants grown continuously in short days flowered after producing 31.4±1.6 (SD) nodes while plants grown continuously in long days did not flower and produced 172.5±9.5 nodes after one year. At various ages, expressed as number of leaves that were at least 1.0 cm in length above the most basal 10-cm leaf, one of three treatments was performed on plants grown from seed in short days: 1) whole plants were shifted from short days to long days, 2) the terminal bud was removed and then rooted and grown in long days, and 3) the terminal bud was removed and then rooted and grown in short days. Whole plants flowered only when shifted from short days to long days at age 15 or later. Only rooted terminal buds from plants at age 15 or older produced plants that flowered when grown in long days. Only terminal buds from plants at age 15 or older that were rooted and grown in short days produced the same number of nodes as they would have produced in their original locations while buds from younger plants produced more nodes than they would have in their original locations. Thus, determination for floral development in the terminal bud, as assayed by rooting, is simultaneous with the commitment to flowering as assayed by shifting whole plants to non-inductive conditions.
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  • 4
    ISSN: 1573-5028
    Keywords: aspartate aminotransferase ; cDNA ; soybean ; isozyme ; mitochondria ; antibodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A soybean leaf cDNA clone, pSAT2, was isolated by hybridization to a carrot aspartate aminotransferase (EC 2.6.1.1.; AAT) cDNA clone at low stringency. pSAT2 contained an open reading frame encoding a 47640 Da protein. The protein encoded by pSAT2 showed significant sequence similarity to AAT proteins from both plants and animals. It was most similar to two Panicum mitochondrial AATs, 81.5% and 82.0% identity. Alignment of the pSAT2-encoded protein with other mature AAT enzymes revealed a 25 amino acid N-terminal extension with characteristics of a mitochondrial transit peptide. A plasmid, pEXAT2, was constructed to encode the mature pSAT2 protein lacking the putative mitochondrial transit peptide. Escherichia coli containing the plasmid expressed a functional AAT isozyme which comigrated with the soybean AAT4 isozyme during agarose gel electrophoresis. Equilibrium sucrose gradient sedimentation of soybean extracts demonstrated that AAT4 specifically cofractionated with mitochondria. Antibodies raised against the pEXAT2-encoded AAT protein reacted with AAT4 of soybean and not with other AAT isozymes detected in soybean tissues, providing further evidence that clone pSAT2 encodes the soybean mitochondrial isozyme AAT4.
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  • 5
    ISSN: 1573-5028
    Keywords: aspartate aminotransferase ; cDNA ; glyoxysome ; isozyme ; peroxisomal targeting signal ; soybean
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A soybean cDNA clone, pSAT1, which encodes both the cytosolic and glyoxysomal isozymes of aspartate aminotransferase (AAT; EC 2.6.1.1) was isolated. Genomic Southern blots and analysis of genomic clones indicated pSAT1 was encoded by a single copy gene. pSAT1 contained an open reading frame with ca. 90% amino acid identity to alfalfa and lupin cytosolic AAT and two in-frame start codons, designated ATG1 and ATG2. Alignment of this protein with other plant cytosolic AAT isozymes revealed a 37 amino acid N-terminal extension with characteristics of a peroxisomal targeting signal, designated PTS2, including the modified consensus sequence RL-X5-HF. The second start codon ATG2 aligned with previously reported start codons for plant cytosolic AAT cDNAs. Plasmids constructed to express the open reading frame initiated by each of the putative start codons produced proteins with AAT activity in Escherichia coli. Immune serum raised against the pSAT1-encoded protein reacted with three soybean AAT isozymes, AAT1 (glyoxysomal), AAT2 (cytosolic), and AAT3 (subcellular location unknown). We propose the glyoxysomal isozyme AAT1 is produced by translational initiation from ATG1 and the cytosolic isozyme AAT2 is produced by translational initiation from ATG2. N-terminal sequencing of purified AAT1 revealed complete identity with the pSAT1-encoded protein and was consistent with the processing of the PTS2. Analysis of cytosolic AAT genomic sequences from several other plant species revealed conservation of the two in-frame start codons and the PTS2 sequence, suggesting that these other species may utilize a single gene to generate both cytosolic and glyoxysomal or peroxisomal forms of AAT.
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  • 6
    Publication Date: 1990-08-01
    Print ISSN: 0733-222X
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Springer Nature
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  • 7
    Publication Date: 1987-12-01
    Print ISSN: 0032-0935
    Electronic ISSN: 1432-2048
    Topics: Biology
    Published by Springer
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