Activation of Archaeal Transcription by Recruitment of the TATA-Binding Protein

The hyperthermophilic archaeon Methanococcus jannaschii encodes two putative transcription regulators, Ptr1 and Ptr2, that are members of the Lrp/AsnC family of bacterial transcription regulators. In contrast, this archaeon's RNA polymerase and core transcription factors are of eukaryotic type....

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2003-04, Vol.100 (9), p.5097-5102
Hauptverfasser: Ouhammouch, Mohamed, Dewhurst, Robert E., Hausner, Winfried, Thomm, Michael, Geiduschek, E. Peter
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container_end_page 5102
container_issue 9
container_start_page 5097
container_title Proceedings of the National Academy of Sciences - PNAS
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creator Ouhammouch, Mohamed
Dewhurst, Robert E.
Hausner, Winfried
Thomm, Michael
Geiduschek, E. Peter
description The hyperthermophilic archaeon Methanococcus jannaschii encodes two putative transcription regulators, Ptr1 and Ptr2, that are members of the Lrp/AsnC family of bacterial transcription regulators. In contrast, this archaeon's RNA polymerase and core transcription factors are of eukaryotic type. Using the M. jannaschii high-temperature in vitro transcription system, we show that Ptr2 is a potent transcriptional activator, and that it conveys its stimulatory effects on its cognate eukaryal-type transcription machinery from an upstream activating region composed of two Ptr2-binding sites. Transcriptional activation is generated, at least in part, by Ptr2-mediated recruitment of the TATA-binding protein to the promoter.
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subjects Archaea
Bacteria
Base Sequence
Binding sites
Biological Sciences
DNA
DNA Primers
Hydroxyl Radical
Intergenic DNA
Methanococcus - genetics
Methanococcus - metabolism
Promoter Regions, Genetic
Proteins
Regulator genes
Ribonucleic acid
RNA
TATA box
TATA-Box Binding Protein - physiology
Transcription factors
Transcriptional activation
Transcriptional Activation - physiology
Transcriptional regulatory elements
title Activation of Archaeal Transcription by Recruitment of the TATA-Binding Protein
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