View Item 

Show simple item record

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

dc.contributor.authorJørgensen, Casper M.en_US
dc.contributor.authorFields, Christopher J.en_US
dc.contributor.authorChander, Preethien_US
dc.contributor.authorWatt, Desmonden_US
dc.contributor.authorBurgner, John W.en_US
dc.contributor.authorSmith, Janet L.en_US
dc.contributor.authorSwitzer, Robert L.en_US
dc.date.accessioned2012-03-16T15:59:53Z
dc.date.available2012-03-16T15:59:53Z
dc.date.issued2008-02en_US
dc.identifier.citationJørgensen, Casper M. ; Fields, Christopher J.; Chander, Preethi; Watt, Desmond; Burgner, John W.; Smith, Janet L.; Switzer, Robert L. (2008). " pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein â characterization and regulation by uridine and guanosine nucleotides." FEBS Journal 275(4). <http://hdl.handle.net/2027.42/90317>en_US
dc.identifier.issn1742-464Xen_US
dc.identifier.issn1742-4658en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/90317
dc.publisherWiley Periodicals, Inc.en_US
dc.publisherBlackwell Publishing Ltden_US
dc.subject.otherRNA Binding to Proteinsen_US
dc.subject.otherUltracentrifugationen_US
dc.subject.otherRegulation of Attenuationen_US
dc.subject.otherPyrRen_US
dc.subject.otherPyrimidine Nucleotidesen_US
dc.titlepyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein – characterization and regulation by uridine and guanosine nucleotidesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationum Life Sciences Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, USAen_US
dc.contributor.affiliationother Bindley Bioscience Center, Purdue University, West Lafayette, IN, USAen_US
dc.contributor.affiliationother Department of Biological Sciences, Purdue University, Lafayette, IN, USAen_US
dc.contributor.affiliationother Department of Biochemistry, University of Illinois, Urbana, USAen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90317/1/FEBS_6227_sm_FigsS1-S5.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/90317/2/j.1742-4658.2007.06227.x.pdf
dc.identifier.doi10.1111/j.1742-4658.2007.06227.xen_US
dc.identifier.sourceFEBS Journalen_US
dc.identifier.citedreferenceGagyi C, Burcurenci N, Sirbu O, Labesse G, Ionescu M, Ofiteru A, Assairi L, Landais S, Danchin A, Barzu O et al. ( 2003 ) UMP kinase from the Gram‐positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity. Eur J Biochem 270, 3196 – 3204.en_US
dc.identifier.citedreferenceTurner RJ, Lu Y. & Switzer RL ( 1994 ) Regulation of the Bacillus subtilis pyrimidine biosynthetic ( pyr ) gene cluster by an autogenous transcriptional attenuation mechanism. J Bacteriol 176, 3708 – 3722.en_US
dc.identifier.citedreferenceLu Y, Turner RJ & Switzer RL ( 1995 ) Roles of the three transcriptional attenuators of the Bacillus subtilis pyrimidine biosynthetic operon in the regulation of its expression. J Bacteriol 177, 1315 – 1325.en_US
dc.identifier.citedreferenceGhim S‐Y & Switzer RL ( 1996 ) Characterization of cis ‐acting mutations in the first attenuator region of the B. subtilis pyr operon that are defective in regulation of expression by pyrimidines. J Bacteriol 178, 2351 – 2355.en_US
dc.identifier.citedreferenceGhim S‐Y & Switzer RL ( 1996 ) Mutations in B. subtilis PyrR, the pyr regulatory protein with defects in regulation by pyrimidines. FEMS Microbiol Lett 137, 13 – 18.en_US
dc.identifier.citedreferenceTomchick DR, Turner RJ, Switzer RL & Smith JL ( 1998 ) Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a bifunctional pyr RNA‐binding attenuation protein and uracil phosphoribosyltransferase. Structure 6, 337 – 350.en_US
dc.identifier.citedreferenceLu Y & Switzer RL ( 1996 ) Transcriptional attenuation of the Bacillus subtilis pyr operon by the PyrR regulatory protein and uridine nucleotides in vitro. J Bacteriol 178, 7206 – 7211.en_US
dc.identifier.citedreferenceChander P, Halbig KM, Miller JK, Fields CJ, Bonner HKS, Grabner GK, Switzer RL & Smith JL ( 2005 ) Structure of the nucleotide complex of PyrR, the pyr attenuation protein from Bacillus caldolyticus, suggests dual regulation by pyrimidine and purine nucleotides. J Bacteriol 187, 1773 – 1782.en_US
dc.identifier.citedreferenceChander P ( 2006 ) Structural analysis of the regulatory protein of pyrimidine biosynthesis, PyrR. PhD Thesis, Purdue University, West Lafayette, IN.en_US
dc.identifier.citedreferenceGhim S‐Y, Nielsen P & Neuhard J ( 1994 ) Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus. J Gen Microbiol 140, 479 – 491.en_US
dc.identifier.citedreferenceGhim S‐Y & Neuhard J ( 1994 ) The pyrimidine biosynthesis operon of the thermophile Bacillus caldolyticus includes genes for uracil phosphoribosyltransferase and uracil permease. J Bacteriol 176, 3698 – 3707.en_US
dc.identifier.citedreferenceWong L & Lohmann TM ( 1993 ) A double‐filter method for nitrocellulose‐filter binding: application to protein‐nucleic acid interactions. Proc Nat Acad Sci USA 90, 5428 – 5432.en_US
dc.identifier.citedreferenceSchuch R, Garibian A, Saxild HH, Piggot PJ & Nygaard P ( 1999 ) Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm‐pupG operon. Microbiology (Reading) 145, 2957 – 2966.en_US
dc.identifier.citedreferenceSchuck P. ( 2003 ) On the analysis of protein self‐association by sedimentation velocity analytical ultracentrifugation. Anal Biochem 320, 104 – 124.en_US
dc.identifier.citedreferenceBalbo A, Minor KH, Velikovsky CA, Mariuzza RA, Peterson CB & Schuck P ( 2005 ) Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation. Proc Nat Acad Sci USA 102, 81 – 86.en_US
dc.identifier.citedreferenceMøllgaard H & Neuhard J ( 1978 ) Deoxycytidylate deaminase from Bacillus subtilis. J Biol Chem 253, 3536 – 3542.en_US
dc.identifier.citedreferenceSaxild HH & Nygaard P ( 1991 ) Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools. J Gen Microbiol 137, 2387 – 2394.en_US
dc.identifier.citedreferenceBernlohr DA & Switzer RL ( 1983 ) Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase inactivation in vivo. J Bacteriol 153, 937 – 949.en_US
dc.identifier.citedreferencePaulus TJ & Switzer RL ( 1979 ) Synthesis and inactivation of the carbamyl phosphate synthetase isozymes of Bacillus subtilis during growth and sporulation. J Bacteriol 140, 769 – 773.en_US
dc.identifier.citedreferenceWillemöes M & Sigurskjold BW ( 2002 ) Steady‐state kinetics of the glutaminase reaction of CTP synthase from Lactococcus lactis. the role of the allosteric activator GTP in coupling between glutamine hydrolysis and CTP synthesis. Eur J Biochem 19, 4772 – 4779.en_US
dc.identifier.citedreferenceKrasny L & Gourse RL ( 2004 ) An alternative strategy for bacteria ribosome synthesis: Bacillus subtilis rRNA transcription regulation. EMBO J 23, 4473 – 4483.en_US
dc.identifier.citedreferenceLopez JM, Dromerick A & Freese E ( 1981 ) Response of guanosine 5’‐triphosphate concentration to nutritional changes and its significance for Bacillus subtilis sporulation. J Bacteriol 146, 605 – 613.en_US
dc.identifier.citedreferenceRatnayake‐Lecamwasam M, Serror P, Wong KW & Sonenshein AL ( 2001 ) Bacillus subtilis CodY represses early‐stationary‐phase genes by sensing GTP levels. Genes Dav 15, 1093 – 1103.en_US
dc.identifier.citedreferenceSchaak JE, Yakhnin H, Bevilqcqua PC & Babitzke P ( 2003 ) A Mg 2+ ‐dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding. J Mol Biol 332, 555 – 574.en_US
dc.identifier.citedreferenceLaue TM, Shah BD, Ridgeway TM & Pelletier SL ( 1992 ) Computer‐aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science ( Harding SE, Rowe AJ & Horton JC eds), pp. 90 – 125. The Royal Society of Chemistry, Cambridge, UK.en_US
dc.identifier.citedreferenceDurschlag H & Zipper P ( 1997 ) Calculation of partial specific volumes and other volumetric properties of small molecules and polymers. J Appl Cryst 30, 803 – 807.en_US
dc.identifier.citedreferenceSchuck P ( 2000 ) Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78, 1606 – 1619.en_US
dc.identifier.citedreferencePerbal B & Herve G ( 1972 ) Biosynthesis of Escherichia coli aspartate transcarbamylase I. parameters of gene expression and sequential biosynthesis of the subunits. J Mol Biol 70, 511 – 529.en_US
dc.identifier.citedreferenceZuker M ( 2003 ) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31, 3406 – 3415.en_US
dc.identifier.citedreferenceSwitzer RL, Turner RJ & Lu Y ( 1999 ) Regulation of the Bacillus subtilis pyrimidine biosynthetic operon by transcriptional attenuation: control of gene expression by an mRNA‐binding protein. Prog Nucl Acids Res Mol Biol 62, 329 – 367.en_US
dc.identifier.citedreferenceBonner ER, D’Elia JN, Billips BK & Switzer RL ( 2001 ) Molecular recognition of pyr mRNA by the Bacillus subtilis attenuation regulatory protein PyrR. Nucleic Acids Res 29, 4851 – 4865.en_US
dc.identifier.citedreferenceTurner RJ, Bonner ER, Grabner GK & Switzer RL ( 1998 ) Purification and characterization of Bacillus subtilis PyrR, a bifunctional pyr mRNA‐binding attenuation protein/uracil phosphoribosyltransferase. J Biol Chem 273, 5932 – 5938.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Name:
FEBS_6227_sm_FigsS1-S5.pdf
Size:
3.319MB
Format:
PDF
View/Open
Name:
j.1742-4658.2007.06227.x.pdf
Size:
475.7KB
Format:
PDF
View/Open

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.