In the closed form of RfaH (right), the C-terminal domain (CTD, blue) and the N-terminal domain (NTD, green) are close to each other. The alpha-helical CTD masks the area of the NTD which binds to the RNA polymerase. Binding to a specific piece of DNA results in domain separation (left) which in turn leads to the complete refolding of the CTD. In this state, the NTD can bind RNA polymerase and the CTD can bind ribosomal protein S10. RfaH is thus a regulatory component of the transcription of DNA into RNA.
Image: Dr. Stefan Knauer, University of Bayreuth; free for publication only when reference is included.
"Never before has such a fundamental structural change been observed for proteins", Prof. Paul Rösch notes. "This result is spectacular as we were able to simultaneously elucidate the structural transition and its functional consequences for central cellular processes in bacteria." RfaH's ability to change its structure enables regulation of the translation of bacterial genetic information into proteins (gene expression).Regulatory functions of the domains in gene expression
Christian Wißler | Universität Bayreuth
Further reports about: > Bio-Macromolecules > CTD > DNA > NTD > RNA > RNA polymerase > RfaH > Translation > amino acid > bacterial pathogens > bacterial protein > building block > cellular process > genetic information > magnetic resonance > magnetic resonance spectroscopy > molecular process > molecular structure > three-dimensional structure > transcription
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