H-NS, one of the most abundant proteins in Escherichia coli, is able to condense the DNA and to act as a transcriptional repressor of many genes [1]. The protein consists of an N-ter- minal protein oligomerization domain and a C-terminal DNA-binding domain separated by a linker. Oligomerization allows HN-S to bind to multiple sites on the DNA, thereby regulating the activity of many different genes. The peculiar features of the interaction of the C-domain of H-NS with a target DNA fragment have been illustrated in a previous article [2]. Here we show the structure of the complex between the C-domain of H-NS and a target DNA fragment 20 base pairs in length and discuss the main features of this interaction. We show that H-NS binds to the minor groove of DNA through a loop previously characterized by NMR titration experiments.
Solution structure of H-NS C-terminal domain bound to its target DNA
SPURIO, Roberto;MIANO, Antonino;GUALERZI, Claudio;
2014-01-01
Abstract
H-NS, one of the most abundant proteins in Escherichia coli, is able to condense the DNA and to act as a transcriptional repressor of many genes [1]. The protein consists of an N-ter- minal protein oligomerization domain and a C-terminal DNA-binding domain separated by a linker. Oligomerization allows HN-S to bind to multiple sites on the DNA, thereby regulating the activity of many different genes. The peculiar features of the interaction of the C-domain of H-NS with a target DNA fragment have been illustrated in a previous article [2]. Here we show the structure of the complex between the C-domain of H-NS and a target DNA fragment 20 base pairs in length and discuss the main features of this interaction. We show that H-NS binds to the minor groove of DNA through a loop previously characterized by NMR titration experiments.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
