1SG5

Solution structure of Yaeo, a Rho-specific inhibitor of transcription termination

Summary for 1SG5

• Entry DOI: 10.2210/pdb1sg5/pdb
• Descriptor: orf, hypothetical protein (1 entity in total)
• Functional Keywords: a+b protein, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, transcription, protein binding
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 9708.90

Authors

Gutierrez, P.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2004-02-23, release date: 2005-07-12, Last modification date: 2024-05-22)

Primary citation

Gutierrez, P.,Kozlov, G.,Gabrielli, L.,Elias, D.,Osborne, M.J.,Gallouzi, I.E.,Gehring, K.
Solution Structure of YaeO, a Rho-specific Inhibitor of Transcription Termination
J.Biol.Chem., 282:23348-23353, 2007

PubMed Abstract: Rho-dependent transcription termination is an essential process for the regulation of bacterial gene expression. Thus far, only two Rho-specific inhibitors of bacterial transcription termination have been described, the psu protein from the satellite bacteriophage P4 and YaeO from Escherichia coli. Here, we report the solution structure of YaeO, the first of a Rho-specific inhibitor of transcription termination. YaeO is an acidic protein composed of an N-terminal helix and a seven-stranded beta sandwich. NMR chemical shift perturbation experiments revealed that YaeO binds proximal to the primary nucleic acid binding site of Rho. Based on the NMR titrations, a docked model of the YaeO-Rho complex was calculated. These results suggest that YaeO binds outside the Rho hexamer, acting as a competitive inhibitor of RNA binding. In vitro gel shift assays confirmed the inhibition of nucleic acid binding to Rho. Site-directed mutagenesis showed that the negative character of YaeO is essential for its function in vivo.

PubMed: 17565995
DOI: 10.1074/jbc.M702010200

Experimental method

SOLUTION NMR