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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 55 (1983), S. 161-163 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 51 (2004), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Protein splicing inteins can be small as ∼130 aa or up to ∼600 aa when harbouring an endonuclease domain. Here we report the identification and characterization of an unusually large intein, 1650 aa long and the largest of known inteins, encoded by the replicative DNA helicase gene dnaB of the oceanic N2-fixing cyanobacterium Trichodesmium erythraeum. This Ter DnaB-1 intein co-exists with a 177-aa mini-intein in the same host protein and harbours large tandem repeats in which an 84-aa sequence is repeated 16 times. Comparison between this tandem repeats and the recently reported tandem repeats of Ter DnaE-1 intein revealed differences and similarities. The two tandem repeats, residing in different inteins of different host proteins, differ by 50% in size and have little sequence similarity. Tandem repeats in the Ter DnaB-1 intein were required for the protein splicing activity when tested in Escherichia coli, in contrast to tandem repeats of the Ter DnaE-1 intein that inhibited protein splicing. On the other hand, tandem repeats of both inteins are located in the same corresponding region of the intein sequence and have the same number of repeating units. These suggest that the two tandem repeats could be related but have diverged greatly in size, sequence and effect on protein splicing. Alternatively, they could have independent origins but evolved certain similarities because of common constraints in structure and maintenance.
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 34 (2000), S. 61-76 
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Intein is the protein equivalent of intron and has been discovered in increasing numbers of organisms and host proteins. A self-splicing intein catalyzes its own removal from the host protein through a posttranslational process of protein splicing. A mobile intein displays a site-specific endonuclease activity that confers genetic mobility to the intein through intein homing. Recent findings of intein structure and the mechanism of protein splicing illuminated how inteins work and yielded clues regarding intein's origin, spread, and evolution. Inteins can evolve into new structures and new functions, such as split inteins that do trans-splicing. The structural basis of intein function needs to be identified for a full understanding of the origin and evolution of this marvelous genetic element.
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  • 4
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 68 (1996), S. 850-852 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Si ions were implanted into thermally grown SiO2 films on crystalline Si at an energy of 120 keV and with a dose of 1016 cm−2. Under an ultraviolet excitation of ∼5.0 eV, the implanted films exhibit blue luminescence with a peak of ∼2.7 eV at room temperature. The blue emission is caused by oxygen vacancies in the films. © 1996 American Institute of Physics.
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 166 (1984), S. 248-252 
    ISSN: 0014-5793
    Keywords: ATP-dependent protease ; Chloroplast ; Chloroplast biogenesis ; Protein regulation ; Protein synthesis
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-5028
    Keywords: Chlamydomonas ; chloroplast ; ribosome ; translational regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two mutants of the green alga Chlamydomonas reinhardtii, one deficient in the small subunit of the chloroplast ribosome and the other having chloroplast ribosomes with reduced function under certain conditions, show a characteristic syndrome of photosynthetic defects resulting from reduced chloroplast protein synthesis. These include subnormal levels of ribulose 1,5-bisphosphate carboxylase (Rubisco), reduced Hill reaction activity, diminished capacity to fix CO2, and abnormal thylakoid stacking. However, these mutants accumulate normal appearing chloroplast ribosome monomers or large subunits containing normal ribosomal protein components. In this paper, we demonstrate that pulse-labeled cells of these mutants synthesize two large subunit chloroplast ribosomal proteins at about 60% of the wild-type rate, whereas Rubisco large subunit (LSU) and the alpha subunit of CF1 are made at only 4 to 8% of the wild-type rate. No difference in the rate of turnover between ribosomal proteins and Rubisco LSU in mutant and wild-type cells was observed during a subsequent 60 min chase. Differences between the mutants and wild-type cells in the relative synthesis rates of these proteins were not reflected in the relative levels of mRNA (either hybridizable or in vitro translatable). In aggregate, these data suggest that C. reinhardtii preferentially translates chloroplast ribosomal protein mRNAs under conditions of reduced total chloroplast protein synthesis.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 18 (1992), S. 985-988 
    ISSN: 1573-5028
    Keywords: Fe-binding protein ; NifH-like protein ; cytochrome b6/f complex ; tRNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 34 (1997), S. 339-343 
    ISSN: 1573-5028
    Keywords: chloroplast ; DNA bending ; DNA binding ; HU-like protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Guillardia theta chloroplast hlpA gene encodes a protein resembling bacterial histone-like protein HU. This gene was cloned and overexpressed in Escherichia coli cells, and the resulting protein product, HlpA, was purified and characterized in vitro. In addition to exhibiting a general DNA-binding activity, the chloroplast HlpA protein also strongly facilitated cyclization of a short DNA fragment in the presence of T4 DNA ligase, indicating its ability to mediate very tight DNA curvatures.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 23 (1993), S. 297-308 
    ISSN: 1573-5028
    Keywords: Chlamydomonas ; chlB gene ; chlorophyll synthesis ; chloroplast genome ; gene disruption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Light-independent chlorophyll synthesis occurs in some algae, lower plants, and gymnosperms, but not in angiosperms. We have identified a new chloroplast gene, chlB, that is required for the light-independent accumulation of chlorophyll in the green alga Chlamydomonas reinhardtii. The chlB gene was cloned, sequenced, and then disrupted by performing particle gun-mediated chloroplast transformation. The resulting homoplasmic mutant was unable to accumulate chlorophyll in the dark and thus exhibited a ‘yellow-in-the-dark’ phenotype. The chlB gene encodes a polypeptide of 688 amino acid residues, and is distinct from two previously characterized chloroplast genes (chlN and chlL) also required for light-independent chlorophyll accumulation in C. reinhardtii. Three unidentified open reading frames in chloroplast genomes of liverwort, black pine, and Chlamydomonas moewusii were also identified as chlB genes, based on their striking sequence similarities to the C. reinhardtii chlB gene. A chlB-like gene is absent in chloroplast genomes of tobacco and rice, consistent with the lack of light-independent chlorophyll synthesis in these plants. Polypeptides encoded by the chloroplast chlB genes also show significant sequence similarities with the bchB gene product of Rhodobacter capsulatus. Comparisons among the chloroplast chlB and the bacterial bchB gene products revealed five highly conserved sequence areas that are interspersed by four stretches of highly variable and probably insertional sequences.
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  • 10
    ISSN: 1617-4623
    Keywords: Ribosomal protein S4 ; Streptomycin dependence ; Chloroplast ribosomes ; Ribosomal protein S12
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ribosomal protein gene rps4 was cloned and sequenced from the chloroplast genome of Chlamydomonas reinhardtii. The N-terminal 213 amino acid residues of the S4 protein are encoded in the single-copy region (SCR) of the genome, while the C-terminal 44 amino acid residues are encoded in the inverted repeat (IR). The deduced 257 amino acid sequence of C. reinhardtii S4 is considerably longer (by 51–59 residues) than S4 proteins of other photosynthetic species and Escherichia coli, due to the presence of two internal insertions and a C-terminal extension. A short conserved C-terminal motif found in all other S4 proteins examined is missing from the C. reinhardtii protein. In E. coli, mutations in the S4 protein suppress the streptomycin-dependent (sd) phenotype of mutations in the S12 protein. Because we have been unable to identify similar S4 mutations among suppressors of an sd mutation in C. reinhardtii S12 obtained using UV mutagenesis, we made site-directed mutations [Arg68 (CGT) to Len (CTG and CTT)] in the wild-type rps4 gene equivalent to an E. coli Gln53 to Len ribosomal ambiguity mutation (ram), which suppresses the sd phenotype and decreases translational accuracy. These mutants were tested for their ability to transform the sd S 12 mutation of C. reinhardtii to streptomycin independence. The streptomycin-independent isolates obtained by biolistic transformation all possessed the original sd mutation in rps12, but none had the expected donor Leu68 mutations in rps4. Instead, six of 15 contained a Gln73 (CAA) to Pro (CCA) mutation five amino acids downstream from the predicted mutant codon, irrespective of rps4 donor DNA. Two others contained six- and ten-amino acid, in-frame insertions at S4 positions 90 and 92 that appear to have been induced by the biolistic process itself. Eight streptomycin-independent isolates analyzed had wild-type rps4 genes and may possess mutations identical to previously isolated suppressors of sd that define at least two additional chloroplast loci. Cloned rps4 genes from streptomycin-independent isolates containing the Gln73 to Pro mutation and the 6-amino acid insertion in r-protein S4 transform the sd strain to streptomycin independence.
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