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  • 1
    Electronic Resource
    Electronic Resource
    Protein Binding to Expanded Telomere Repeats in Tetrahymena thermophila (2003)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 50 (2003), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . The ends of eukaryotic chromosomes are protected by DNA-protein structures called telomeres. Telomeric DNA is highly conserved, usually consisting of long tracts of a repeating G-rich sequence. Tetrahymena thermophila telomeric DNA consists of alternating blocks of GGGG and TT sequences (i.e. a G4T2 repeat sequence). We examined the relative importance of the guanine and thymine elements of the repeat sequence in promoting in vitro binding by T. thermophila proteins. We identified single- and, for the first time, double-stranded telomere binding activities from a crude T. thermophila protein extract and tested the binding of these activities to altered telomere repeat sequences. All deletions or substitutions made to the guanine element virtually abolished binding, indicating that four G's are essential for recognition by the binding activity. However, G's alone are not sufficient for efficient binding, as elimination of the thymine element dramatically reduced binding. By contrast, substantial expansion of the thymine element was well tolerated, even though one such change, G4T4, is lethal in vivo. We tested up to a four-fold expansion of the thymine element and found that highly efficient binding was still achieved. These results suggest a minimal recognition sequence for T. thermophila proteins, with the T element providing an important spacer between essential G elements. demonstrate some flexibility in the binding of many telomere proteins, because the variant sequences tested often contain more than one base change, the minimal changes that permit or disrupt binding cannot be deduced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.2003.tb00146.x
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  • 2
    Electronic Resource
    Electronic Resource
    cDNA structure and expression patterns of a low-temperature-specific wheat gene tacr7 (1997)
    Springer
    Plant molecular biology 34 (1997), S. 643-650 
    Details
    ISSN: 1573-5028
    Keywords: callus ; crown tissue ; gene expression ; low temperature ; wheat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The low-temperature (2 °C)-specific wheat cDNA, pTACR7, represents a gene designated tacr7 from hard red winter wheat (HRWW; Triticum aestivum L. cv. Winoka). The term low-temperature-specific (LTS) is used because tacr7 is not induced by ABA or stresses such as salt, dehydration, and heat. pTACR7 was isolated by RT-PCR with mRNA from wheat crown tissue, the oligonucleotide primers derived from the barley cognate pHVCR8 (GenBank accession number L28091). Based on the deduced amino acid sequence, TACR7 is highly hydrophobic, with a single transmembrane domain and an amino acid bias for leucine (19%). Thus, the encoded protein TACR7 is unique among low-temperature-regulated wheat proteins described in the literature. Analysis of steady-state levels of tacr7 transcripts (630 nt) showed accumulation in wheat seedlings, crown tissue, and callus cultures after transfer from control (25 °C) to low temperature (2 °C). No detectable transcripts were observed by northern blot hybridization with pTACR7 probe from seedling or callus treated with ABA, salt, dehydration, or heat stress. tacr7 transcripts accumulated during 2 °C exposure to a greater amount in a freeze-resistant HRWW (FR; SDmut 16029) than in a freeze-susceptible HRWW (FS; SDmut 16169) crown tissue, with the largest difference between genotypes being 30% ± 3% at 3 weeks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005852703506
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