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  • 1
    Electronic Resource
    Electronic Resource
    Translational regulation of mRNAs for ribosomal proteins during early Drosophila development (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 5798-5803 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00342a017
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  • 2
    Electronic Resource
    Electronic Resource
    Transgenic anopheline mosquitoes impaired in transmission of a malaria parasite (2002)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 417 (2002), S. 452-455 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Malaria is estimated to cause 0.7 to 2.7 million deaths per year, but the actual figures could be substantially higher owing to under-reporting and difficulties in diagnosis. If no new control measures are developed, the malaria death toll is projected to double in the next 20 years. Efforts to ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/417452a
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  • 3
    Electronic Resource
    Electronic Resource
    Evolution of Chitin-Binding Proteins in Invertebrates (1999)
    Springer
    Journal of molecular evolution 48 (1999), S. 341-347 
    Details
    ISSN: 1432-1432
    Keywords: Key words: Chitin binding — Peritrophic matrix — Chitinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Analysis of a group of invertebrate proteins, including chitinases and peritrophic matrix proteins, reveals the presence of chitin-binding domains that share significant amino acid sequence similarity. The data suggest that these domains evolved from a common ancestor which may be a protein containing a single chitin-binding domain. The duplication and transposition of this chitin-binding domain may have contributed to the functional diversification of chitin-binding proteins. Sequence comparisons indicated that invertebrate and plant chitin binding domains do not share significant amino acid sequence similarity, suggesting that they are not coancestral. However, both the invertebrate and the plant chitin-binding domains are cysteine-rich and have several highly conserved aromatic residues. In plants, cysteines have been elucidated in maintaining protein folding and aromatic amino acids in interacting with saccharides [Wright HT, Sanddrasegaram G, Wright CS (1991) J Mol Evol 33:283–294]. It is likely that these residues perform similar functions in invertebrates. We propose that the invertebrate and the plant chitin-binding domains share similar mechanisms for folding and saccharide binding and that they evolved by convergent evolution. Furthermore, we propose that the disulfide bonds and aromatic residues are hallmarks for saccharide-binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00006478
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  • 4
    Electronic Resource
    Electronic Resource
    Initiation of Haemoglobin Synthesis by Methionyl-tRNA (1970)
    [s.l.] : Nature Publishing Group
    Nature 227 (1970), S. 913-918 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The synthesis of haemoglobin in a cell free system containing yeast tRNA is initiated by a specific methionine tRNA. Another methionine tRNA responds to internal codons in the messenger. The initiating methionine is removed from the nascent protein to leave valine as the terminal amino-acid, but ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/227913a0
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  • 5
    Electronic Resource
    Electronic Resource
    Abrupt decline in the rate of accumulation of total protein and yolk in postvitellogenic egg chambers ofDrosophila (1983)
    Springer
    Development genes and evolution 192 (1983), S. 189-195 
    Details
    ISSN: 1432-041X
    Keywords: Drosophila melanogaster ; Embryo Metabolism ; Protein biosynthesis ; Ovary ; Growth and development egg yolk
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The accumulation of endogenously synthesized non-yolk proteins, and of exogenously derived yolk, was quantitated during oogenesis and embryogenesis ofDrosophila. Rates of non-yolk protein accumulation were calculated, and were correlated with polysome content at each developmental stage. Three distinct phases of non-yolk protein accumulation were observed: 1) relatively slow accumulation, lasting to stage 9 of oogenesis; 2) very rapid accumulation between stages 10 and 12 of oogenesis, when half of the protein of the mature egg is accumulated in less than 4 h; and 3) no further protein accumulation from stage 12 of oogenesis through at least the gastrula stage of embryogenesis. During phases 1 and 2, rates of non-yolk protein accumulation correlate well with the polysome content of egg chambers. Surprisingly, during the entire phase 3 the content of polysomes remains at high levels, even though no detectable protein accumulation occurs. This finding is in agreement with the low levels of protein synthesis that have been measured during early embryogenesis, and strongly suggests that late in oogenesis the efficiency of translation suddenly drops by about 20-fold. Moreover, our results imply that polysome content cannot always be directly correlated with protein synthetic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00848689
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  • 6
    Electronic Resource
    Electronic Resource
    Overproduction and translational regulation of rp49 ribosomal protein mRNA in transgenic Drosophila carrying extra copies of the gene (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 171-175 
    Details
    ISSN: 1617-4623
    Keywords: Drosophila development ; Ribosomal proteins ; Translational regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary During Drosophila early development the translation of ribosomal protein mRNAs is regulated specifically and coordinately. In this study we assayed for changes of ribosomal protein rp49 gene expression in flies transformed with extra copies of the gene. RNA blot analysis revealed that the rp49 transcript was overrepresented in most of the transformed fly lines: flies carrying three times more genes than the wild type contained up to seven times more mRNA. The abundance of other ribosomal protein mRNAs was not affected. Despite the large differences in rp49 mRNA content, the proportion of the rp49 mRNA which was associated with polysomes during oogenesis and early embryogenesis did not differ significantly from the wild type, implying that rp49 protein is overproduced in the transgenic flies. The results indicate that the basis for coordinate r-protein gene expression lies in the intrinsic properties of r-protein genes, rather than in a dynamic system that separately modulates the expression of individual genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00261717
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  • 7
    Electronic Resource
    Electronic Resource
    Identification and germline transformation of the ribosomal protein rp21 gene of Drosophila: Complementation analysis with the Minute QIII locus reveals nonidentity (1988)
    Springer
    Molecular genetics and genomics 213 (1988), S. 354-358 
    Details
    ISSN: 1617-4623
    Keywords: Drosophila ; Minute ; Ribosomal protein ; Transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Minute loci represent a class of about 50 different Drosophila genes that appear to be functionally related. These genes may code for components of the protein synthetic apparatus. While one Minute locus has been recently shown to code for a ribosomal protein, it is not yet known whether any of the other Minute loci also code for ribosomal proteins. We have addressed this question by a combined molecular and genetic approach. In this report, a cloned DNA encoding the ribosomal protein rp21 is partially characterized. The rp21 gene maps to the same region (region 80 of chromosome 3L) as the temperature-sensitive Minute QIII gene. Using P-element mediated transformation, the rp21 gene was transformed into the germline of Drosophila. RNA blot experiments revealed that the transformed gene is expressed in transgenic flies. However, genetic complementation analysis indicated that the QIII locus and the rp21 gene are not identical. Implications of these findings for the relationship between Minutes and ribosomal protein genes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00339602
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  • 8
    Electronic Resource
    Electronic Resource
    Generation of Minute phenotypes by a transformed antisense ribosomal protein gene (1992)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 13 (1992), S. 256-263 
    Details
    ISSN: 0192-253X
    Keywords: Minute mutations ; oogenesis ; Drosophila ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Antisense RNAs have been used for gene interference experiments in many cell types and organisms. However, relatively few experiments have been conducted with antisense genes integrated into the germ line. In Drosophila reduced ribosomal protein (r-protein) gene function has been hypothesized to result in a Minute phenotype. In this report we examine the effects of antisense r-protein 49 expression, a gene known to correspond to a Minute mutation An antisense rp49 gene driven by a strong and inducible promoter was transformed into the Drosophila germ line. Induction of this gene led to the development of flies with weak Minute phenotypes and to the transient arrest of oogenesis. Parameters that may affect the success of antisense gene inactivation are discussed. © 1992 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020130403
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