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Full-Text Articles in Life Sciences
Reproductive Structure And Organogenesis In A Cottonwood, Populus Deltoides (Salicaceae), Robert B. Kaul
Reproductive Structure And Organogenesis In A Cottonwood, Populus Deltoides (Salicaceae), Robert B. Kaul
School of Biological Sciences: Faculty Publications
The organogenesis of inflorescences, flowers, and fruits was followed for two years in a male and a female tree of eastern cottonwood, Populus deltoides. Soon after anthesis, an inflorescence for the next year is initiated as a continuation of the apical meristem in most axillary buds of the extension shoot of the current year. Bract and then floral primordia arise helically, and by the end of summer all floral appendages are evident. Individual perianth parts are evident early in ontogeny but not at anthesis; they are vascularized independently by distal traces of discrete vascular strands that also serve the …
Purification, Characterization, And Submitochondrial Localization Of A 58-Kilodalton Nad(P)H Dehydrogenase, Michael H. Luethy, Jay J. Thelen, Andrew F. Knudten, Thomas Elthon
Purification, Characterization, And Submitochondrial Localization Of A 58-Kilodalton Nad(P)H Dehydrogenase, Michael H. Luethy, Jay J. Thelen, Andrew F. Knudten, Thomas Elthon
School of Biological Sciences: Faculty Publications
An NADH dehydrogenase activity from red beet (Beta vulgaris 1.) root mitochondria was purified to a 58-kD protein doublet. An immunologically related dehydrogenase was partially purified from maize (Zea mays L. 873) mitochondria to a 58-kD protein doublet, a 45-kD protein, and a few other less prevalent proteins. Polyclonal antibodies prepared against the 58-kD protein of red beet roots were found to immunoprecipitate the NAD(P)H dehydrogenase activity. The antibodies cross-reacted to similar proteins in mitochondria from a number of plant species but not to rat liver mitochondrial proteins. The polyclonal antibodies were used in conjunction with maize mitochondrial fractionation to …
The Majority Of Yeast Upf1 Co-Localizes With Polyribosomes In The Cytoplasm, Audrey L. Atkin, Nicola Altamura, Peter Leeds, Michael R. Culbertson
The Majority Of Yeast Upf1 Co-Localizes With Polyribosomes In The Cytoplasm, Audrey L. Atkin, Nicola Altamura, Peter Leeds, Michael R. Culbertson
School of Biological Sciences: Faculty Publications
In Saccharomyces cerevisiae the UPF1 protein is required for nonsense-mediated mRNA
decay, the accelerated turnover of mRNAs containing a nonsense mutation. Several lines
of evidence suggest that translation plays an important role in the mechanism of
nonsense mRNA decay, including a previous report that nonsense mRNAs assemble in
polyribosomes. In this study we show that UPF1 and ribosomal protein Li co-localize in
the cytoplasm and that UPF1 co-sediments with polyribosomes. To detect UPF1, three
copies of the influenza hemagglutinin epitope were placed at the C-terminus. The tagged
protein, UPF1-3EP, retains 86% (± 5%) of function. Using immunological detection, we
found …
Rna Determinants Of Junction Site Selection In Rna Virus Recombinants And Defective Interfering Rnas, K. Andrew White, Thomas Jack Morris
Rna Determinants Of Junction Site Selection In Rna Virus Recombinants And Defective Interfering Rnas, K. Andrew White, Thomas Jack Morris
School of Biological Sciences: Faculty Publications
RNA recombination plays an important role in the diversification and evolution of RNA viruses. Most of these events are believed to be mediated by an actively copying viral replicase switching from a donor template to an acceptor template, where it resumes synthesis. In addition, Intramolecular replicase-mediated events (I.e., rearrangements) can lead to the generation of replicable deleted forms of a viral genome, termed defective interfering (DI) RNAs. To gain further insight into the recombination process, the effect of various primary and secondary structures on recombination site selection in vivo was examined using plant RNA tombusviruses. The effect of sequence Identity …
Isolation, Sequencing, And Analysis Of A 14-3-3 Brain Protein Homolog From Pea (Pisum Sativum L.), Bratislav Stankovic, Ana Garit-Stankovic, Christopher M. Smith, Eric Davies
Isolation, Sequencing, And Analysis Of A 14-3-3 Brain Protein Homolog From Pea (Pisum Sativum L.), Bratislav Stankovic, Ana Garit-Stankovic, Christopher M. Smith, Eric Davies
School of Biological Sciences: Faculty Publications
Initially identified as acidic, homodimeric proteins abundantly and preferentially present in mammalian brain neurotransmitter complexes, the eukaryotic 14-3-3 homologs appear to be ubiquitous and highly conserved among highly diverse organisms, including Xenopus, Drosophila, and Saccharomyces (Aitken et al., 1992). They have also been isolated, cloned, and sequenced from various plants, such as Arabidopsis (Lu et al., 1992), Oenotkera, Spinacea (Hirsch et al., 1992), Zea (De Vetten et al., 1992), Lycopersicon (Laughner et al., 19941, Hordeum (Brandt et al., 19921, and Oyza (Kidou et al., 1993). Although there are no available sequence data in the GenBank (version 94-5), immunoprecipitation experiments suggest …