The Bacterial Regulatory Protein H-NS A Versatile Modulator of Nucleic Acid Structures
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Oliver Schröder
Abstract
The small DNA binding protein HNS is attracting broad interest for its profound involvement in the regulation of bacterial physiology. It is involved in the regulation of many genes in response to a changing environment and functions in the adaptation to many different kinds of stress. Many HNScontrolled genes, including the hns gene itself, are further linked to global regulatory networks. HNS thus plays a key role in maintaining bacterial homeostasis under conditions of a rapidly changing environment. In this review we summarize recent results from combined biochemical and biophysical efforts which have yielded new insights into the threedimensional structure and function of HNS. The protein consists of two distinct domains separated by an unstructured linker region, and the structural details available today have helped to understand how these domains may interact with each other or with ligand molecules. Functional studies have, in addition, revealed mechanistic clues for the various HNS activities, like temperature or growth phasedependent regulation. Important elements for the specific regulatory activities of HNS comprise different modes of DNA binding, protein oligomerization, the competition with other regulators and the fact that the topology of the target DNA is modulated during complex formation. The distinctive ability to recognize nucleic acid structures in combination with other proteins also explains HNSdependent posttranscriptional activities where the interaction with defined RNA structures and the interference with RNA/protein complexes during mRNA translation are crucial for regulation. Thus, protein/protein interactions, in combination with the recognition and modulation of nucleic acid structures, are key elements of the different mechanisms which make HNS such a versatile regulator.
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Highlight: Environmental Mutagenesis
- DNA Double-Strand Break Repair by Homologous Recombination
- An Overview of the Analysis of DNA Methylation in Mammalian Genomes
- Methylation of the RASSF1A Gene in Human Cancers
- Exocyclic DNA Adducts as Oxidative Stress Markers in Colon Carcinogenesis: Potential Role of Lipid Peroxidation, Dietary Fat and Antioxidants
- DNA Polymorphisms as Modulators of Genotoxicity and Cancer
- Recent Aspects of Oxidative DNA Damage: Guanine Lesions, Measurement and Substrate Specificity of DNA Repair Glycosylases
- The Bacterial Regulatory Protein H-NS A Versatile Modulator of Nucleic Acid Structures
- Molecular Mechanisms of Nickel Carcinogenesis
- DNA Binding Properties of the Yeast Msh2-Msh6 and Mlh1-Pms1 Heterodimers
- N-Hydroxyarylamine O-Acetyltransferase-Deficient Escherichia coli Strains Are Resistant to the Mutagenicity of Nitro Compounds
- Functional Genomics of C190T Single Nucleotide Polymorphism in Human N-Acetyltransferase 2
- Increase in Ceramide Level Alters the Lysosomal Targeting of Cathepsin D prior to Onset of Apoptosis in HT-29 Colon Cancer Cells
- Reconstitution of Transport-Active Multidrug Resistance Protein 2 (MRP2; ABCC2) in Proteoliposomes
- Processing of the Human Transferrin Receptor at Distinct Positions within the Stalk Region by Neutrophil Elastase and Cathepsin G
- Analysis of the Prion Protein in Primates Reveals a New Polymorphism in Codon 226 (Y226F)
- Inducibility of the Streptomyces traRts107-Ptra Expression Cassette in Mycobacterium smegmatis
