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  • Bacillus thuringiensis  (1)
  • Humans  (1)
  • Maximum parsimony  (1)
  • 1990-1994  (3)
  • 1960-1964
  • 1991  (3)
  • 1961
  • 1
    ISSN: 1573-5028
    Keywords: Bacillus thuringiensis ; cry genes ; insecticidal crystal protein ; protoplast electroporation ; RNA stability ; transgenic tobacco
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have examined expression of several insecticidal crystal protein (ICP) genes of Bacillus thuringiensis in transgenic tobacco plants and electroporated carrot protoplasts. We determined that low levels of lepidopteran toxin cryIA(b) ICP gene expression in plants and electroporated carrot cells is due to RNA instability. We used a series of 3′ deleted cryIA(b) constructs directed by the cauliflower mosaic virus 35S promoter to demonstrate that this instability is minimally contained in the first 579 bases of the gene in both systems. This instability may result from 5′ → 3′ as well as 3′ → 5′ RNA metabolism. The coleopteran toxic cryIIIA gene was also examined in electroporated carrot cells, and found to be poorly expressed. A model for improvement of ICP RNA stability in plants is presented.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5133
    Keywords: Molecular phylogeny ; Maximum parsimony ; Chondrichthyes ; Dipnoi ; Actinopterygii ; Tetrapoda ; Sarcopterygii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Synopsis Approximately 98% of the sequence of the 18S ribosomal RNA (rRNA) of the coelacanth Latimeria chalumnae was determined by a combination of direct RNA sequencing and sequencing of rRNA genes amplified by the polymerase chain reaction. This sequence was compared with 18S rRNA sequences of similar length from seven other vertebrate species, representing the taxa Petromyzontiformes, Holocephali, Elasmobranchii, Actinopterygii, Dipnoi, Amphibia, and Amniota, in order to determine the most likely sister group of the coelacanth. Maximum parsimony analysis of these sequences resulted in a single most parsimonious tree containing a number of anomalous relationships among these groups. A bootstrap analysis showed that none of the relationships in this tree was significantly supported at the 95% level, however. Addition of data from 15 other vertebrates (providing multiple representatives of most of the higher taxa) resulted in similar ambiguous groupings, as did a number of methods of editing the sites compared (designed to eliminate rapidly evolving positions). These results may be due to a relatively rapid radiation of the major lineages of osteichthyans, the resolution of which will require molecular information from a larger portion of the coelacanth genome.
    Type of Medium: Electronic Resource
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1991-05-24
    Description: The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupas, A -- Van Dyke, M -- Stock, J -- AI20980/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1162-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031185" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/chemistry ; Animals ; Databases, Factual ; Humans ; Probability ; *Protein Conformation ; Proteins/chemistry/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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