Abstract
The nucleoid-associated protein H-NS is thought to play an essential role in the organization of bacterial chromatin in Escherichia coli. Homologues, often with very low sequence identity, are found in most gram-negative bacteria. Microscopic analysis reveals that, despite limited sequence identity, their structural organization results in similar DNA binding properties.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / physiology
-
Consensus Sequence
-
DNA, Bacterial / chemistry*
-
DNA-Binding Proteins / chemistry*
-
DNA-Binding Proteins / physiology
-
Escherichia coli Proteins / chemistry*
-
Escherichia coli Proteins / physiology
-
Microscopy, Atomic Force
-
Molecular Chaperones / chemistry*
-
Molecular Chaperones / physiology
-
Protein Binding
-
Trans-Activators / chemistry*
-
Trans-Activators / physiology
Substances
-
Bacterial Proteins
-
DNA, Bacterial
-
DNA-Binding Proteins
-
Escherichia coli Proteins
-
H-NS protein, bacteria
-
Molecular Chaperones
-
MvaT protein, Pseudomonas
-
StpA protein, E coli
-
Trans-Activators