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  • 1
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Escherichia coli DnaK, DnaJ and GrpE are required for renaturation of heat-inactivated λ CI857 repressor (Gaitanaris et al., 1990). Here we demonstrate that in addition to the above three proteins, GroEL and GroES are necessary for the CI857 repressor to acquire full activity at the permissive temperature. Although full-length soluble repressor is present at normal amounts, the protein has reduced specific activity and migrates abnormally on native gels. To determine where the different chaperones act in protein folding, we identified their cellular locations. DnaK and DnaJ are associated with nascent polypeptide chains in translating ribosomes. In contrast, GroEL, although it is transiently associated with newly synthesized proteins, is absent from the ribosomes. This suggests that DnaK and DnaJ ptay an early role in protein maturation, whereas GroEL acts at a later stage.
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  • 2
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Escherichia coli nusG gene product is required for transcription termination by phage HK022 Nun protein at the λnutR site in vivo. We show that it is also essential for Nun termination at λnutL. Three recessive missense nusG mutations have been isolated that inhibit termination by Nun at λnutR. The mutations are ineffective in a λpL nutL fusion, even when λnutR replaces λnutL. The mutant strains support λ growth, indicating that λ N antitermination activity is not impaired. Transcription arrest by Nun in vitro is stimulated by NusG protein at both λnutR and λnutL. Mutant NusG protein fails to enhance transcriptional arrest by Nun at either site. The mutant protein, like the wild-type protein, suppresses transcriptional pausing by RNA polymerase and stimulates Rho-dependent termination. These results imply that the role of NusG in Nun termination may be distinct from its roles in other transcription reactions.
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  • 3
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 292 (1981), S. 212-215 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The nusA1 and nusB5 mutations result in a partial suppression of polarity and thus transcription termination in Escherichia coli. As these mutations block the transcription antitermination activity of bacteriophage λN gene product, they paradoxically seem to enhance transcription termination ...
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  • 4
    Electronic Resource
    Electronic Resource
    Osney Mead, Oxford OX2 0EL, UK : Blackwell Scientific Publication
    Molecular microbiology 17 (1995), S. 0 
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Escherichia coli NusG protein binds Rho in vitro and is required for efficient Rho-dependent transcription termination in vivo. In this work we examine transcription termination in cells that overexpress NusG. Termination at the Rho-dependent λtL1 and λtR1 sites was significantly inhibited by excess NusG, whereas the Rho-independent λtl site was fully functional. Although Western analysis showed no reduction in the levels of soluble Rho, termination was restored when Rho was also overexpressed. Our data indicate that the ratio of NusG and Rho proteins affects the efficiency of transcription termination.
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  • 5
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract HK022 is a temperate coliphage related to phage lamba. Its chromosome has been completely sequenced, and several aspects of its life cycle have been intensively studied. In the overall arrangement, expression, and function of most of its genes, HK022 broadly resembles lamba and other members of the lamba family. Upon closer view, significant differences emerge. The differences reveal alternative strategies used by related phages to cope with similar problems and illuminate previously unknown regulatory and structural motifs. HK022 prophages protect lysogens from superinfection by producing a sequence-specific RNA binding protein that prematurely terminates nascent transcripts of infecting phage. It uses a novel RNA-based mechanism to antiterminate its own early transcription. The HK022 protein shell is strengthened by a complex pattern of covalent subunit interlinking to form a unitary structure that resembles chainmail armor. Its integrase and repressor proteins are similar to those of lamba, but the differences provide insights into the evolution of biological specificity and the elements needed for construction of a stable genetic switch.
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