The nuclear matrix attachment DNA (MAR) binding protein SATB1 is a
sequence context-specific binding protein that binds in the minor
groove, making virtually no contact with the DNA bases. The SATB1
binding sites consist of a special AT-rich sequence context in which
one strand is well-mixed A's, T's, and C's, excluding G's (ATC sequences),
which is typically found in clusters within different MARs. To determine
the extent of conservation of the SATB1 gene among different species,
we cloned a mouse homolog of the human STAB1 cDNA from a cDNA expression
library of the mouse thymus, the tissue in which this protein is
predominantly expressed. This mouse cDNA encodes a 764-amino-acid
protein with a 98\% homology in amino acid sequence to the human
SATB1 originally cloned from testis. To characterize the DNA binding
domain of this novel class of protein, we used the mouse SATB1 cDNA
and delineated a 150-amino-acid polypeptide as the binding domain.
This region confers full DNA binding activity, recognizes the specific
sequence context, and makes direct contact with DNA at the same nucleotides
as the whole protein. This DNA binding domain contains a novel DNA
binding motif: when no more than 21 amino acids at either the N-
or C-terminal end of the binding domain are deleted, the majority
of the DNA binding activity is lost. The concomitant presence of
both terminal sequences is mandatory for binding. These two terminal
regions consist of hydrophilic amino acids and share homologous sequences
that are different from those of any known DNA binding motifs. We
propose that the DNA binding region of SATB1 extends its two terminal
regions toward DNA to make direct contact with DNA.
La Jolla Cancer Research Foundation, California 92037.
journal
Mol Cell Biol
number
3
pages
1852--1860
volume
14
pmid
8114718
timestamp
2008.09.25
file
:C\:\\Users\\denilw\\Desktop\\Steven Jones Lab\\Papers\\SatB1\\A novel
DNA-binding motif in the nuclear matrix attachment DNA-binding protein
SATB1.pdf:PDF
%0 Journal Article
%1 Nakagomi1994
%A Nakagomi, K.
%A Kohwi, Y.
%A Dickinson, L. A.
%A Kohwi-Shigematsu, T.
%D 1994
%J Mol Cell Biol
%K Acid Acid; Alignment; Amino Analysis; Animals; Antigens, Attachment Binding Cloning, Complementary, DNA DNA, DNA-Binding Data; Deletion; Deoxyribonucleoproteins, Factors, Genes; Gland, Homology, Matrix Matrix, Mice; Molecular Molecular; Mutational Nuclear Nuclear; Oligodeoxyribonucleotides, Protein; Proteins, Proteins; Region Relationship; Sequence Sequence; Sites; Structure-Activity TATA-Box Thymus Transcription chemistry chemistry/metabolism; chemistry; genetics; metabolism;
%N 3
%P 1852--1860
%T A novel DNA-binding motif in the nuclear matrix attachment DNA-binding
protein SATB1.
%V 14
%X The nuclear matrix attachment DNA (MAR) binding protein SATB1 is a
sequence context-specific binding protein that binds in the minor
groove, making virtually no contact with the DNA bases. The SATB1
binding sites consist of a special AT-rich sequence context in which
one strand is well-mixed A's, T's, and C's, excluding G's (ATC sequences),
which is typically found in clusters within different MARs. To determine
the extent of conservation of the SATB1 gene among different species,
we cloned a mouse homolog of the human STAB1 cDNA from a cDNA expression
library of the mouse thymus, the tissue in which this protein is
predominantly expressed. This mouse cDNA encodes a 764-amino-acid
protein with a 98\% homology in amino acid sequence to the human
SATB1 originally cloned from testis. To characterize the DNA binding
domain of this novel class of protein, we used the mouse SATB1 cDNA
and delineated a 150-amino-acid polypeptide as the binding domain.
This region confers full DNA binding activity, recognizes the specific
sequence context, and makes direct contact with DNA at the same nucleotides
as the whole protein. This DNA binding domain contains a novel DNA
binding motif: when no more than 21 amino acids at either the N-
or C-terminal end of the binding domain are deleted, the majority
of the DNA binding activity is lost. The concomitant presence of
both terminal sequences is mandatory for binding. These two terminal
regions consist of hydrophilic amino acids and share homologous sequences
that are different from those of any known DNA binding motifs. We
propose that the DNA binding region of SATB1 extends its two terminal
regions toward DNA to make direct contact with DNA.
@article{Nakagomi1994,
abstract = {The nuclear matrix attachment DNA (MAR) binding protein SATB1 is a
sequence context-specific binding protein that binds in the minor
groove, making virtually no contact with the DNA bases. The SATB1
binding sites consist of a special AT-rich sequence context in which
one strand is well-mixed A's, T's, and C's, excluding G's (ATC sequences),
which is typically found in clusters within different MARs. To determine
the extent of conservation of the SATB1 gene among different species,
we cloned a mouse homolog of the human STAB1 cDNA from a cDNA expression
library of the mouse thymus, the tissue in which this protein is
predominantly expressed. This mouse cDNA encodes a 764-amino-acid
protein with a 98\% homology in amino acid sequence to the human
SATB1 originally cloned from testis. To characterize the DNA binding
domain of this novel class of protein, we used the mouse SATB1 cDNA
and delineated a 150-amino-acid polypeptide as the binding domain.
This region confers full DNA binding activity, recognizes the specific
sequence context, and makes direct contact with DNA at the same nucleotides
as the whole protein. This DNA binding domain contains a novel DNA
binding motif: when no more than 21 amino acids at either the N-
or C-terminal end of the binding domain are deleted, the majority
of the DNA binding activity is lost. The concomitant presence of
both terminal sequences is mandatory for binding. These two terminal
regions consist of hydrophilic amino acids and share homologous sequences
that are different from those of any known DNA binding motifs. We
propose that the DNA binding region of SATB1 extends its two terminal
regions toward DNA to make direct contact with DNA.},
added-at = {2008-09-25T22:07:47.000+0200},
author = {Nakagomi, K. and Kohwi, Y. and Dickinson, L. A. and Kohwi-Shigematsu, T.},
biburl = {https://www.bibsonomy.org/bibtex/28ee18783e62005655793de70b19359ef/denilw},
file = {:C\:\\Users\\denilw\\Desktop\\Steven Jones Lab\\Papers\\SatB1\\A novel
DNA-binding motif in the nuclear matrix attachment DNA-binding protein
SATB1.pdf:PDF},
institution = {La Jolla Cancer Research Foundation, California 92037.},
interhash = {e39354f6384ab0d3c295e415f166e1e6},
intrahash = {8ee18783e62005655793de70b19359ef},
journal = {Mol Cell Biol},
keywords = {Acid Acid; Alignment; Amino Analysis; Animals; Antigens, Attachment Binding Cloning, Complementary, DNA DNA, DNA-Binding Data; Deletion; Deoxyribonucleoproteins, Factors, Genes; Gland, Homology, Matrix Matrix, Mice; Molecular Molecular; Mutational Nuclear Nuclear; Oligodeoxyribonucleotides, Protein; Proteins, Proteins; Region Relationship; Sequence Sequence; Sites; Structure-Activity TATA-Box Thymus Transcription chemistry chemistry/metabolism; chemistry; genetics; metabolism;},
month = Mar,
number = 3,
owner = {denilw},
pages = {1852--1860},
pmid = {8114718},
timestamp = {2008-09-25T22:07:48.000+0200},
title = {A novel DNA-binding motif in the nuclear matrix attachment DNA-binding
protein SATB1.},
volume = 14,
year = 1994
}