Аннотация
SATB1 is a transcriptional regulator controlling the gene expression
that is essential in the maturation of the immune T-cell. SATB1 binds
to the nuclear matrix attachment regions of DNA, where it recruits
histone deacetylase and represses transcription through a local chromatin
remodeling. Here we determined the solution structure of the matrix
attachment region-binding domain, possessing similarity to the CUT
DNA-binding domain, of human SATB1 by NMR spectroscopy. The structure
consists of five alpha-helices, in which the N-terminal four are
arranged similarly to the four-helix structure of the CUT domain
of hepatocyte nuclear factor 6alpha. By an NMR chemical shift perturbation
analysis and by surface plasmon resonance analyses of SATB1 mutant
proteins, an interface for DNA binding was revealed to be located
at the third helix and the surrounding regions. Surface plasmon resonance
experiments using groove-specific binding drugs and methylated DNAs
indicated that the domain recognizes DNA from the major groove side.
These observations suggested that SATB1 possesses a DNA-binding mode
similar to that of the POU-specific DNA-binding domain, which is
known to share structural similarity to the four-helix CUT domain.
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