[NMR paper] Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.

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Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.

Related Articles Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.

FEBS J. 2013 Apr 20;

Authors: Renault M, García J, Cordeiro TN, Baldus M, Pons M

Abstract
Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes that respond to environmental changes in osmolarity, pH or temperature. H-NS oligomerization is essential for its activity. Structural models from different truncated forms are available. However, high-resolution structural details of full-length protein H-NS and its DNA bound state have largely remained elusive. We report on progress to characterize the biologically active H-NS oligomers using solid-state NMR spectroscopy (ssNMR). We have compared uniformly ((13) C,(15) N)-labeled ssNMR preparations of the isolated N-terminal region (H-NS 1-47) and full-length H-NS (H-NS 1-137). In both cases, we obtained ssNMR spectra of good quality and characteristic of well-folded proteins. Analysis of two- and three-dimensional ((13) C,(13) C) and ((15) N,(13) C) correlation experiments conducted at high field led to assignments of residues located in different topological regions of the free full-length H-NS protein. These findings confirm that the structure of the (N-terminal) dimerization domain is conserved in the oligomeric full-length protein. Small changes in the dimerization interface suggested by localized chemical shift variations between solution and solid-state spectra may be relevant for DNA recoginition. This article is protected by copyright. All rights reserved.


PMID: 23601147 [PubMed - as supplied by publisher]



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