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  • 1
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] We have signifcantly improved the use of pharmaceutical type capsules as a coating system for the production of synthetic seeds. The capsule body was covered on its inner surface by a watertight film, composed of polyvinyl chloride (PVC), polyvhiyl acetate (PVA) and bentone as a thickener, to ...
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  • 2
    ISSN: 1573-5028
    Keywords: α-prolamin ; kafirin ; monocot gene expression ; transgenic tobacco ; zein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sequences corresponding to 855 bp of 5′ promoter region and the transit peptide from ⋋GK.1, a genomic clone encoding a 22 kDa α-kafirin seed protein from sorghum, were translationally fused to a cloned β-glucuronidase (GUS) coding sequence from uidA and transferred to tobacco via Agrobacterium tumefaciens-mediated transformation. No GUS expression was detectable at any stage of growth in stems or leaves of these plants. However, GUS expression was detected in both embryo and endosperm tissues of resulting tobacco seeds 10–15 days after flowering. Dissected tissues indicate endosperm expression was localized within the bulk endosperm and not within the parenchyma cell layer underlying the integument. These studies also demonstrate that within dissected tobacco embryos, expression from the kafirin promoter was restricted to the mesocotyl region.
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  • 3
    ISSN: 1573-5028
    Keywords: monocot gene expression ; root-specific gene expression ; transgenic rice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two cDNA clones (RCc2 and RCc3) corresponding to mRNAs highly expressed only in root tissues of rice (Oryza sativa L.) seedlings were characterized. Respectively, they encode polypeptides of 146 (14.5 kDa) and 133 amino acids (13.4 kDa) that share high (〈70%) sequence similarity with a polypeptide encoded by a cDNA (ZRP3) encoding an mRNA preferentially expressed in young maize roots. Genomic DNA blot analysis revealed that they are members of a small gene family and RCg2, the gene corresponding to RCc2, was isolated. A 1656 bp 5′-upstream sequence of RCg2 was translationally fused to a β-glucuronidase (GUS) reporter gene and stable introduction of the chimeric construct into rice was confirmed by PCR and genomic DNA blot analyses. Histochemical analysis of transgenic rice plants containing the full-length chimeric gene showed high levels of GUS activity in mature cells and the elongation and maturation zones of primary and secondary roots, and in the root caps, but no GUS activity was detected in root meristematic regions. Surprisingly, high GUS activity was also detected in leaves of the same plants. This raises the possibility that the RCg2 5′-upstream element may not be sufficient for the proper spatial control of root specificity in transgenic rice.
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  • 4
    ISSN: 1573-5028
    Keywords: kafirin ; prolamin ; seed storage protein ; sorghum genomic library ; zein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Electrophoretic analysis of translation products of polyadenylated RNA isolated from mid-maturation sorghum seed in the presence of [35S]met, [3H]leu, or [3H]val revealed two major proteins of kDa and 21 kDa. These products were not detected when [3H]lys was supplied as the radioactive substrate. Under similar electrophoretic conditions, kafirin (a major seed storage prolamin of sorghum), migrated as two bands of 22 kDa and 19 kDa. Sequence analysis of two cDNA clones (pSK8 and pSKR2) from sorghum seed mRNA revealed them to be highly homologous with each other and to the 22 kDa zeins from maize, suggesting that they represented kafirin cDNAs. Compared with pSKR2, pSK8 had an insertion of 24 nucleotides and a deletion of 24 nucleotides, so that the coding regions were nearly identical in length. The deduced amino acid sequence for these cDNA clones reveals that kafirin, like zein, is rich in glutamine and nonpolar amino acids, but contains no lysine. Both kafirin and zein have a 21 amino acid signal peptide exhibiting 80% homology and eight copies of a repetitive amino acid block in the C-terminal domain with the consensus: infI supP LL finP supA LN infQ supP LALANPAAYLQQQQ. The kafirin cDNAs were used as probes to screen a sorghum genomic library; one genomic clone (λGK.1) was sequenced and found to be very similar (97.8%) to the pSK8 cDNA clone. Clone λGK.1 contains features typical for a functional gene in that the intronless open reading frame encoding 268 amino acids is flanked at the 5′ end by sequences corresponding to the CAAT and TATA promoter boxes (positioned at about −60 and −30 bp, respectively, from the transcriptional initiation site), and at the 3′ end by a consensus polyadenylation signal. In common with zein genomic clones, kafirin clones contain a 15 basepair consensus sequence centered at postion −320 relative to the transcriptional initiation site. Under similar hybridization conditions, genomic reconstruction analysis using an oligonucleotide probe indicated the presence of less than 20 copies of kafirin per haploid sorghum genome compared with approximatley 140 copies of zein per haploid maize genome.
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  • 5
    ISSN: 1573-5028
    Keywords: biotin ; embryogenesis ; LEA ; pea ; seed germination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Seeds of Pisum sativum contain a biotinyl polypeptide called SBP65 that behaves as a putative sink for the free vitamin, representing more than 90% of the total protein-bound biotin in mature seeds. A cDNA encoding SBP65 was cloned and sequenced. The deduced primary structure of the protein was confirmed by protein sequencing. Peptide sequencing also indicated binding of the biotin to lysine 103. The biotinylation domain of SBP65 differs markedly from that of presently known biotin enzymes. Molecular analysis of the protein sequence reveals an extremely hydrophilic protein containing several repeated motifs. These properties, as well as the temporal and spatial patterns of expression of this protein, suggest that SBP65 belongs to the LEA (late embryogenesis-abundant) group of proteins.
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  • 6
    ISSN: 1573-5028
    Keywords: cyclophilin ; Oryza sativa ; peptidyl-prolylcis-trans isomerase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract cDNA clones were isolated and sequenced that encode two related but distinct rice cyclophilins,Cyp1 andCyp2. The predicted amino acid sequences of each are 72% identical to human T-cell cyclophilin. Genomic DNA gel blot analysis suggests cyclophilins in rice are encoded by a small, 6–10-member gene family. BothCyp1 andCyp2 have seven extra amino acid residues in the N-terminal portion of the proteins that are not found in human or other non-plant cyclophilins, suggesting that this is a characteristic of plant cyclophilins.Cyp2 was expressed as 1000 nt transcripts in leaf and root tissues.Cyp1 was expressed as 800 and 900 nt transcripts. Whereas the 900 nt transcript was present in both root and leaf mRNA, the 800 nt transcript was only detectable in root mRNA. A genomic clone ofCyp2 was isolated, sequenced and shown to lack introns. A single transcriptional start site was identified 27 residues downstream of a putative TATA box. The 5′ end of the transcript was shown to contain a region rich in adenyl residues (27 of 35). This region would not be conducive to secondary structure formation, which raises the possibility thatCyp2 might be preferentially translated during stress conditions.
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