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pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides.

pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides. Research Abstract Details 

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  • pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides. Abstract Text:

    casper m jørgensenCasper M Jørgensen,christopher j fieldsChristopher J Fields,preethi chanderPreethi Chander,desmond wattDesmond Watt,john w burgnerJohn W Burgner,janet l smithJanet L Smith,robert l switzerRobert L Switzer,casper m Casper M ,christopher j fieldsChristopher J Fields,preethi chanderPreethi Chander,desmond wattDesmond Watt,john w burgnerJohn W Burgner,janet l smithJanet L Smith,robert l switzerRobert L Switzer,

    The PyrR protein regulates expression of pyrimidine biosynthetic (pyr) genes in many bacteria. PyrR binds to specific sites in the 5' leader RNA of target operons and favors attenuation of transcription. Filter binding and gel mobility assays were used to characterize the binding of PyrR from Bacillus caldolyticus to RNA sequences (binding loops) from the three attenuation regions of the B. caldolyticus pyr operon. Binding of PyrR to the three binding loops and modulation of RNA binding by nucleotides was similar for all three RNAs. The apparent dissociation constants at 0 degrees C were in the range 0.13-0.87 nm in the absence of effectors; dissociation constants were decreased by three- to 12-fold by uridine nucleotides and increased by 40- to 200-fold by guanosine nucleotides. The binding data suggest that pyr operon expression is regulated by the ratio of intracellular uridine nucleotides to guanosine nucleotides; the effects of nucleoside addition to the growth medium on aspartate transcarbamylase (pyrB) levels in B. subtilis cells in vivo supported this conclusion. Analytical ultracentrifugation established that RNA binds to dimeric PyrR, even though the tetrameric form of unbound PyrR predominates in solution at the concentrations studied.

    pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides. Publishing Authors By Initials

    cm jørgensenCM Jørgensen,cj fieldsCJ Fields,p chanderP Chander,d wattD Watt,jw burgnerJW Burgner,jl smithJL Smith,rl switzerRL Switzer,cm CM ,cj fieldsCJ Fields,p chanderP Chander,d wattD Watt,jw burgnerJW Burgner,jl smithJL Smith,rl switzerRL Switzer,

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    pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: The FEBS journal

    VOLUME: 275

    Page Numbers: 655-70

    Journal Abbreviation: FEBS J.

    ISSN: 1742-464X

    DAY: 8

    MONTH: 01

    YEAR: 2008

    pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides. Information

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    LANGUAGE: eng

    NlmUniqueID: 101229646

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    Grant and Affiliation Information for pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein - characterization and regulation by uridine and guanosine nucleotides.

    AFFILIATION: Department of Biochemistry, University of Illinois, Urbana, USA.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: FEBS J

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