Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda

Proceedings of the National Academy of Sciences of the United States of America
Irena BoninMarkus C Wahl

Abstract

The C terminus of transcription factor NusA from Escherichia coli comprises two repeat units, which bind during antitermination to protein N from phage lambda. To delineate the structural basis of the NusA-lambdaN interaction, we attempted to crystallize the NusA C-terminal repeats in complex with a lambdaN peptide (residues 34-47). The two NusA domains became proteolytically separated during crystallization, and crystals contained two copies of the first repeat unit in contact with a single lambdaN fragment. The NusA modules employ identical regions to contact the peptide but approach the ligand from opposite sides. In contrast to the alpha-helical conformation of the lambdaN N terminus in complex with boxB RNA, residues 34-40 of lambdaN remain extended upon interaction with NusA. Mutational analyses indicated that only one of the observed NusA-lambdaN interaction modes is biologically significant, supporting an equimolar ratio of NusA and lambdaN in antitermination complexes. Solution studies indicated that additional interactions are fostered by the second NusA repeat unit, consistent with known compensatory mutations in NusA and lambdaN. Contrary to the RNA polymerase alpha subunit, lambdaN binding does not stimulate RNA in...Continue Reading

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Citations

Aug 2, 2007·Journal of Applied Genetics·Agnieszka Szalewska-PalaszAlicja Wegrzyn
Dec 16, 2010·The Journal of Biological Chemistry·Jose A HernandezLuis M Rubio
Jun 12, 2009·Nucleic Acids Research·Stefan PraschPaul Rösch
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Sep 1, 2008·EcoSal Plus·Ranjan SenGhazala Muteeb
Apr 25, 2006·Journal of Molecular Biology·Hyeong C KimMax E Gottesman
Nov 2, 2021·Transcription·Nelly Said, Markus C Wahl

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