Interdomain Crosstalk Leads To Control Of NifA Protein Activity In Response To Ammonium Ions In Herbaspirill Um Seropedicae

R.A. Monteiro, E.M. Souza, R. Wassern, M.G. Yates, F.O. Pedrosa, L.S. Chubatsu

Department of Biochemistry, Universidade Federal do ParanĂ¡, Curitiba, PR, Brazil 1. Introduction

Transcriptional activity of the NifA protein of H. seropedicae is controlled by oxygen and ammonium. The mechanism by which this occurs is not yet well understood. The NifA protein comprises three domains; the N-terminal domain that has a putative regulatory function, the central domain has ATPase activity and the C-terminal domain is involved in DNA binding. In this work, we present evidence that the N-terminal domain of the NifA protein of H. seropedicae interacts in vitro with an N-truncated form of the NifA protein, supporting a regulatory NH4+ dependent role for the N-terminal domain.

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