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(Received for publication, October 11, 1996, and in revised form, January 29, 1997)
From the Burnham Institute, La Jolla Cancer Research Center,
La Jolla, California 92037
SATB1 is a cell type-specific nuclear matrix
attachment region (MAR) DNA-binding protein, predominantly expressed in
thymocytes. We identified an atypical homeodomain and two Cut-like
repeats in SATB1, in addition to the known MAR-binding domain. The
isolated MAR-binding domain recognizes a certain DNA sequence context
within MARs that is highly potentiated for base unpairing. Unlike the MAR-binding domain, the homeodomain when isolated binds poorly and with
low specificity to DNA. However, the combined action of the MAR-binding
domain and the homeodomain allows SATB1 to specifically recognize the
core unwinding element within the base-unpairing region. The core
unwinding element is critical for MAR structure, since point mutations
within this core abolish the unwinding propensity of the MAR. The
contribution of the homeodomain is abolished by alanine substitutions
of arginine 3 and arginine 5 in the N-terminal arm of the homeodomain.
Site-directed mutagenesis of the core unwinding element in the 3
Volume 272, Number 17,
Issue of April 25, 1997
pp. 11463-11470
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
MAR
of the immunoglobulin heavy chain gene enhancer revealed the sequence
5-(C/A)TAATA-3 to be essential for the increase in affinity mediated
by the homeodomain. SATB1 may regulate T-cell development and function
at the level of higher order chromatin structure through the critical
DNA structural elements within MARs.
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