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Characterization of the Na⁺-transporting NADH:ubiquinone oxidoreductase (NQR) in Vibrio cholerae Public Deposited

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  • Characterization of the Sodium-Translocating NADH-Ubiquinone Oxidoreductase (NQR) on Vibrio cholerae Metabolism and Virulence Gene Regulation
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  • We previously reported that inhibition of the Na⁺ translocating NADH:ubiquinone oxidoreductase (NQR), either by chemical inhibition or mutation, increased toxT transcription in Vibrio cholerae. In this study, we revealed that the nqr mutant strain showed similar phenotypes as the Escherichia coli NADH dehydrogenase I (nuo) mutant strain (e.g. growth defect after the mid log growth phase and higher acetic acid production). The increased growth and toxT expression in the nqr mutant relative to the wild type strain appears to be growth phase dependent. However, after longer growth, nqr showed lower amounts of cholera toxin production compared to the parent strain. Interestingly, the nqr mutant strain showed a similar level of toxT expression in the presence of L-lactate, which is known to stimulate respiration. Through Biolog® Phenotype Microarray (PM) analysis, we found that the V. cholerae nqr mutant strain had defects in a broad spectrum of metabolism functions, including amino acid, carboxylic acid, phosphorus, and sulfur utilization, indicating an important role of NQR in V. cholerae metabolism. In addition, nqr mutation increased osmotic sensitivity in V. cholerae. Some of the defects identified by PM analysis, including NaCl sensitivity, were restored by the addition of L-lactate.
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  • OSU Undergraduate Research, Innovation, Scholarship & Creativity (URISC); OSU Howard Hughes Medical Institute (HHMI) Undergraduate Summer program
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  • Slide dimensions: 56" x 36"
  • description.provenance : Made available in DSpace on 2012-09-19T23:17:13Z (GMT). No. of bitstreams: 2ASM2012_NQR_Posterfinal-1.pdf: 451652 bytes, checksum: 00336baa12036b0ff2216939a9aa60f8 (MD5)ASM2012_NQR_Posterfinal-1.pptx: 258865 bytes, checksum: eefa47a1e177a3f4681101adac4bf3a4 (MD5) Previous issue date: 2012
  • description.provenance : Submitted by Sara Fassio (fassios@onid.orst.edu) on 2012-09-18T18:26:12ZNo. of bitstreams: 2ASM2012_NQR_Posterfinal-1.pdf: 451652 bytes, checksum: 00336baa12036b0ff2216939a9aa60f8 (MD5)ASM2012_NQR_Posterfinal-1.pptx: 258865 bytes, checksum: eefa47a1e177a3f4681101adac4bf3a4 (MD5)
  • description.provenance : Approved for entry into archive by Deanne Bruner(deanne.bruner@oregonstate.edu) on 2012-09-19T23:17:13Z (GMT) No. of bitstreams: 2ASM2012_NQR_Posterfinal-1.pdf: 451652 bytes, checksum: 00336baa12036b0ff2216939a9aa60f8 (MD5)ASM2012_NQR_Posterfinal-1.pptx: 258865 bytes, checksum: eefa47a1e177a3f4681101adac4bf3a4 (MD5)
  • description.provenance : Submitted by Sara Fassio (fassios@onid.orst.edu) on 2012-09-14T18:45:46ZNo. of bitstreams: 1ASM2012_NQR_Posterfinal-1.pptx: 258865 bytes, checksum: eefa47a1e177a3f4681101adac4bf3a4 (MD5)
  • description.provenance : Rejected by Deanne Bruner(deanne.bruner@oregonstate.edu), reason: Hi Sara,Congratulations on finishing your research! Could you please convert your .pptx to .pdf and also attach it to your submission? You won't have to add all the information again, you can just upload the .pdf along with the .pptx.Thanks,Deanne J. BrunerScholars Archive TechnicianCenter for Digital Scholarship and ServicesOregon State University121 The Valley LibraryCorvallis, OR 97331-4501e-mail: deanne.bruner@oregonstate.eduphone: 541.737.7330 on 2012-09-17T20:28:23Z (GMT)

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