Please use this identifier to cite or link to this item: http://hdl.handle.net/10603/8551
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dc.coverage.spatialDNAen_US
dc.date.accessioned2013-05-06T06:46:37Z-
dc.date.available2013-05-06T06:46:37Z-
dc.date.issued2013-05-06-
dc.identifier.urihttp://hdl.handle.net/10603/8551-
dc.description.abstractThe ArgP protein of Escherichia coli had previously been described variously by different investigators as an inhibitor of oriC-initiated DNA replication, a nucleoid-associated protein and as a transcriptional regulator of genes involved in DNA replication (dnaA, nrdA), osmoregulation and amino acid metabolism (argO, dapB, gdhA and#61531;the last in Klebsiella pneumoniaeand#61533;). In the studies reported in this thesis, promoter-lac fusions were examined in argP+, and#61508;argP and dominant argP (argPd) mutations bearing strains to identify additional ArgP-regulated genes. The genes gdhA, lysP, lysC, lysA, dapD, and asd were newly identified as ArgP-regulated. All were repressed upon Lysine (Lys) supplementation, and in vitro studies demonstrated that ArgP binds to the regulatory regions in a Lys-sensitive manner ( in contrast to the behaviour at argO, where ArgP binding is Lys-insensitive). Unlike previous reports, neither dnaA nor nrdA was ArgP-regulated in vivo, although their regulatory regions did exhibit non-canonical low-affinity binding to ArgP in vitro. ArgP-argO of E. coli and LysG-lysE of Corynebacterium glutamicum are orthologous regulator-target gene pairs. While LysE is an exporter of both arginine (Arg) and Lys whose expression is induced by Arg, Lys, or histidine (His), ArgO exports Arg alone and its expression is activated by Arg but not Lys or His. In studies reported in this thesis, reconstitution of LysG activation of lysE in E. coli was achieved. Neither ArgP nor LysG could regulate expression of the non-cognate targets, but the ArgPd variants -P274S, -S94L -P108S activated lysE expression in E. coli. The activating effects of LysG and ArgPd on lysE were mutually extinguished when both proteins were co-expressed in Arg- or His-supplemented cultures. Compared to native ArgP, these ArgPds exhibited higher affinity of binding to lysE and less DNA bending at both argO and lysE.en_US
dc.format.extent210p.en_US
dc.languageEnglishen_US
dc.relation--en_US
dc.rightsuniversityen_US
dc.titleArgP protein of Escherichia coli: roles in osmoregulation, gene regulation and inter-relationship with LysG of Corynebacterium glutamicumen_US
dc.creator.researcherMarbaniang, Carmelita Nen_US
dc.subject.keywordGlutamateen_US
dc.subject.keywordLysR type of transcriptional regulatoren_US
dc.subject.keywordOsmoregulationen_US
dc.subject.keywordLysine repressionen_US
dc.subject.keywordNucleoid associated proteinen_US
dc.description.noteBibliography p. 193-210 and Synopsis includeden_US
dc.contributor.guideGowrishankar Jen_US
dc.publisher.placeManipalen_US
dc.publisher.universityManipal Universityen_US
dc.publisher.institutionCentre for DNA Fingerprinting and Diagnostics, Hyderabaden_US
dc.date.registered14/07/2007en_US
dc.date.completed26/02/2013en_US
dc.date.awarded27/02/2013en_US
dc.format.dimensions--en_US
dc.format.accompanyingmaterialNoneen_US
dc.type.degreePh.D.en_US
dc.source.inflibnetINFLIBNETen_US
Appears in Departments:Centre for DNA Fingerprinting and Diagnostics, Hyderabad

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02_certificate.pdf49.39 kBAdobe PDFView/Open
03_abstract.pdf20.7 kBAdobe PDFView/Open
04_declaration.pdf49.1 kBAdobe PDFView/Open
05_acknowledgement.pdf70.76 kBAdobe PDFView/Open
06_contents.pdf176.24 kBAdobe PDFView/Open
07_list_of_tables.pdf91.85 kBAdobe PDFView/Open
08_list_of_figures.pdf78.57 kBAdobe PDFView/Open
09_abbreviations.pdf64.03 kBAdobe PDFView/Open
10_chapter1.pdf1.59 MBAdobe PDFView/Open
11_chapter2.pdf405.71 kBAdobe PDFView/Open
12_chapter3-7.pdf4.28 MBAdobe PDFView/Open
13_conclusion.pdf159.85 kBAdobe PDFView/Open
14_summary.pdf195.85 kBAdobe PDFView/Open
15_bibliography.pdf265.58 kBAdobe PDFView/Open


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