TAILIEUCHUNG - Báo cáo khoa học: NrpRII mediates contacts between NrpRI and general transcription factors in the archaeon ¨ Methanosarcina mazei Go1

We report here on the formation of a complex between the two NrpR homologs present inMethanosarcina mazeiGo¨1 and their binding proper-ties to the nifHandglnK1 promoters. Reciprocal co-chromatography dem-onstrated that NrpRI forms stable complexes with NrpRII (at an NrpRI : NrpRII molar ratio of 1 : 3), which are not affected by 2-oxo-glutarate. | NrpRII mediates contacts between NrpRI and general transcription factors in the archaeon Methanosarcina mazei Go1 Katrin Weidenbach Claudia Ehlers Jutta Kock and Ruth A. Schmitz Institut fur Allgemeine Mikrobiologie Christian-Albrechts Universitat zu Kiel Germany Keywords Archaea Methanosarcina mazei transcription regulation NrpR 2-oxoglutarate Correspondence R. A. Schmitz Institut fur Allgemeine Mikrobiologie Universitat Kiel Am Botanischen Garten 1-9 24118 Kiel Germany Fax 49 431 8802194 Tel 49 431 8804334 E-mail rschmitz@ Received 24 June 2010 revised 3 August 2010 accepted 13 August 2010 doi We report here on the formation of a complex between the two NrpR homologs present in Methanosarcina mazei Go1 and their binding properties to the nifH and glnK1 promoters. Reciprocal co-chromatography demonstrated that NrpRI forms stable complexes with NrpRII at an NrpRI NrpRII molar ratio of 1 3 which are not affected by 2-oxo-glutarate. Promoter-binding analyses using DNA-affinity chromatography and electrophoretic gel mobility shift assays verified that NrpRII is not able to bind to either the nifH promoter or the glnK1 promoter except when in complex with NrpRI. Specific binding of NrpRI to the nifH and glnK1 promoters was shown to be highly sensitive to 2-oxoglutarate regardless of whether only NrpRI or NrpRI in complex with NrpRII bound to the promoter. Finally strong interactions between NrpRII and the general transcription factors TATA-binding proteins TBP 1-3 and the general transcription factor TFIIB TFB were demonstrated interactions which are also sensitive to 2-oxoglutarate. On the basis of these findings we propose the following under nitrogen sufficiency NrpRII binds from solution to either the nifH promoter or the glnK1 promoter by simultaneously contacting NrpRI and TBP plus TFB resulting in full repression of transcription whereas under nitrogen limitation increasing 2-oxoglutarate concentrations .

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