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Author (up) Gatenby, A.A.; Boccara, M.; Baulcombe, D.C.; Rothstein, S.J. file  url
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  Title Expression of a wheat alpha-amylase gene in Escherichia coli: recognition of the translational initiation site and the signal peptide Type Journal Article
  Year 1986 Publication Gene Abbreviated Journal Gene  
  Volume 45 Issue 1 Pages 11-18  
  Keywords DNA/genetics; Escherichia coli/genetics; Plant Proteins/*biosynthesis/genetics; Protein Biosynthesis; Protein Processing, Post-Translational; Protein Sorting Signals/metabolism; Recombinant Fusion Proteins/*biosynthesis/genetics/secretion; Recombinant Proteins/*biosynthesis; Species Specificity; Triticum/enzymology/genetics; alpha-Amylases/*biosynthesis/genetics/secretion; beta-Lactamases/genetics  
  Abstract Transcription of a full-length cDNA clone of wheat alpha-amylase using a lac promoter in Escherichia coli results in synthesis of a precursor alpha-amylase polypeptide of the correct size, indicating that translation initiates correctly. Recognition of the plant translational initiation site by E. coli ribosomes is 15-20% as efficient as the ribosome-binding site of the beta-lactamase gene when it is fused to alpha-amylase. The alpha-amylase signal peptide is recognised in E. coli resulting in secretion of the enzyme into the periplasmic space; deletion of the signal peptide prevents secretion. Replacement of the alpha-amylase signal peptide with a beta-lactamase signal peptide also enables the bacterial cell to secrete the enzyme. The presence of the beta-lactamase and the alpha-amylase signal peptides in tandem results in secretion of the enzyme and removal of both signal peptides.  
  Call Number Serial 498  
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Author (up) Hare, J.M.; Adhikari, S.; Lambert, K.V.; Hare, A.E.; Grice, A.N. file  url
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  Title The Acinetobacter regulatory UmuDAb protein cleaves in response to DNA damage with chimeric LexA/UmuD characteristics Type Journal Article
  Year 2012 Publication FEMS Microbiology Letters Abbreviated Journal FEMS Microbiol Lett  
  Volume 334 Issue 1 Pages 57-65  
  Keywords Acinetobacter--enzymology, genetics, radiation effects; Amino Acid Sequence; Bacterial Proteins--chemistry, genetics, metabolism; DNA Damage--radiation effects; DNA-Directed DNA Polymerase--chemistry, genetics, metabolism; Escherichia coli--chemistry, enzymology, genetics, radiation effects; Escherichia coli Proteins--chemistry, genetics, metabolism; Gene Expression Regulation, Bacterial; Molecular Sequence Data; Protein Processing, Post-Translational; Rec A Recombinases--genetics, metabolism; Sequence Alignment; Serine Endopeptidases--chemistry, genetics, metabolism; Ultraviolet Rays  
  Abstract In the DNA damage response of most bacteria, UmuD forms part of the error-prone (UmuD'(2) )C polymerase V and is activated for this function by self-cleavage after DNA damage. However, the umuD homolog (umuDAb) present throughout the Acinetobacter genus encodes an extra N-terminal region, and in Acinetobacter baylyi, regulates transcription of DNA damage-induced genes. UmuDAb expressed in cells was correspondingly larger (24 kDa) than the Escherichia coli UmuD (15 kDa). DNA damage from mitomycin C or UV exposure caused UmuDAb cleavage in both E. coli wild-type and DeltaumuD cells on a timescale resembling UmuD, but did not require UmuD. Like the self-cleaving serine proteases LexA and UmuD, UmuDAb required RecA for cleavage. This cleavage produced a UmuDAb' fragment of a size consistent with the predicted cleavage site of Ala83-Gly84. Site-directed mutations at Ala83 abolished cleavage, as did mutations at either the Ser119 or Lys156 predicted enzymatic residues. Co-expression of the cleavage site mutant and an enzymatic mutant did not allow cleavage, demonstrating a strictly intramolecular mechanism of cleavage that more closely resembles the LexA-type repressors than UmuD. These data show that UmuDAb undergoes a post-translational, LexA-like cleavage event after DNA damage, possibly to achieve its regulatory action.  
  Call Number Serial 491  
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Author (up) Kosova, K.; Vitamvas, P.; Prasil, I.T.; Renaut, J. file  url
openurl 
  Title Plant proteome changes under abiotic stress--contribution of proteomics studies to understanding plant stress response Type Journal Article
  Year 2011 Publication Journal of Proteomics Abbreviated Journal J Proteomics  
  Volume 74 Issue 8 Pages 1301-1322  
  Keywords Arabidopsis/genetics; Cold Temperature/adverse effects; Droughts; Gene Expression Profiling; Herbicides/pharmacology; Hot Temperature/adverse effects; Metals, Heavy/adverse effects; Oryza sativa/genetics; Plant Proteins/*genetics; Plants/*genetics; Protein Processing, Post-Translational; Proteome/*genetics; Stress, Physiological/*genetics  
  Abstract Plant acclimation to stress is associated with profound changes in proteome composition. Since proteins are directly involved in plant stress response, proteomics studies can significantly contribute to unravel the possible relationships between protein abundance and plant stress acclimation. In this review, proteomics studies dealing with plant response to a broad range of abiotic stress factors--cold, heat, drought, waterlogging, salinity, ozone treatment, hypoxia and anoxia, herbicide treatments, inadequate or excessive light conditions, disbalances in mineral nutrition, enhanced concentrations of heavy metals, radioactivity and mechanical wounding are discussed. Most studies have been carried out on model plants Arabidopsis thaliana and rice due to large protein sequence databases available; however, the variety of plant species used for proteomics analyses is rapidly increasing. Protein response pathways shared by different plant species under various stress conditions (glycolytic pathway, enzymes of ascorbate-glutathione cycle, accumulation of LEA proteins) as well as pathways unique to a given stress are discussed. Results from proteomics studies are interpreted with respect to physiological factors determining plant stress response. In conclusion, examples of application of proteomics studies in search for protein markers underlying phenotypic variation in physiological parameters associated with plant stress tolerance are given.  
  Call Number Serial 229  
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Author (up) Strahl, B.D.; Allis, C.D. file  url
openurl 
  Title The language of covalent histone modifications Type Journal Article
  Year 2000 Publication Nature Abbreviated Journal Nature  
  Volume 403 Issue 6765 Pages 41-45  
  Keywords Acetylation; Amino Acid Sequence; Animals; Chromatin/*physiology; Histones/chemistry/metabolism/*physiology; Humans; Lysine/physiology; Microtubules/physiology; Models, Biological; Molecular Sequence Data; Phosphorylation; Protein Processing, Post-Translational; Serine/metabolism  
  Abstract Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a 'histone code' that is, read by other proteins to bring about distinct downstream events.  
  Call Number Serial 1988  
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Author (up) Van de Ven, W.J.; Creemers, J.W.; Roebroek, A.J. file  url
openurl 
  Title Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway Type Journal Article
  Year 1991 Publication Enzyme Abbreviated Journal Enzyme  
  Volume 45 Issue 5-6 Pages 257-270  
  Keywords Animals; Binding Sites; Catalysis; Cloning, Molecular; Drosophila melanogaster; Furin; Humans; Invertebrate Hormones/genetics/metabolism; Mice; Models, Molecular; Multigene Family; Protein Conformation; Protein Precursors/*metabolism; *Protein Processing, Post-Translational; Sequence Homology, Amino Acid; Substrate Specificity; Subtilisins/genetics/*metabolism  
  Abstract Furin, the translational product of the recently discovered fur gene, appears to be the first known mammalian member of the subtilisin family of serine proteases and the first known mammalian proprotein-processing enzyme with cleavage selectivity for paired basic amino acid residues. Structurally and functionally, it resembles the prohormone-processing enzyme, kexin (EC 3.4.21.61), which is encoded by the KEX2 gene of yeast Saccharomyces cerevisiae. Most likely, furin is primarily involved in the processing of precursors of proteins that are secreted via the constitutive secretory pathway. Here, we review the discovery of the fur gene and describe the isolation of cDNA clones corresponding to human and mouse fur and to two fur-like genes of Drosophila melanogaster, Dfur1 and Dfur2. We also compare the structural organization of the various deduced furin proteins to that of yeast kexin, and of other members of the subtilisin family of serine proteases. Furthermore, the biosynthesis of biologically active human and mouse furin is evaluated. Finally, the cleavage specificity for paired basic amino acid residues of human and mouse furin is demonstrated by the correct processing of the precursor for von Willebrand factor.  
  Call Number Serial 524  
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