ARID Transcription Factor Family
Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and
invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including
embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and
of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative
transcriptional regulation and a likely involvement in the modification of chromatin structure. The basic structure of the
ARID domain domain appears to be a series of six alpha-helices separated by beta-strands, loops, or turns, but the
structured region may extend to an additional helix at either or both ends of the basic six. Based on primary sequence
homology, they can be partitioned into three structural classes: Minimal ARID proteins that consist of a core domain formed
by six alpha helices; ARID proteins that supplement the core domain with an N-terminal alpha-helix; and Extended-ARID
proteins, which contain the core domain and additional alpha-helices at their N- and C-termini.
The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity. The ARID
consensus and other structural features are common to both p270 and yeast SWI1, suggesting that p270 is a human counterpart
of SWI1. The approximately 100-residue ARID sequence is present in a series of proteins strongly implicated in the
regulation of cell growth, development, and tissue-specific gene expression. Although about a dozen ARID proteins can be
identified from database searches, to date, only Bright (a regulator of B-cell-specific gene expression), dead ringer (a
Drosophila melanogaster gene product required for normal development), and MRF-2 (which represses expression from the
cytomegalovirus enhancer) have been analyzed directly in regard to their DNA binding properties. Each binds preferentially
to AT-rich sites. In contrast, p270 shows no sequence preference in its DNA binding activity, thereby demonstrating that
AT-rich binding is not an intrinsic property of ARID domains and that ARID family proteins may be involved in a wider range
of DNA interactions.
Members of the recently discovered ARID (AT-rich interaction domain) family of DNA-binding proteins are found in fungi and
invertebrate and vertebrate metazoans. ARID-encoding genes are involved in a variety of biological processes including
embryonic development, cell lineage gene regulation and cell cycle control. Although the specific roles of this domain and
of ARID-containing proteins in transcriptional regulation are yet to be elucidated, they include both positive and negative
transcriptional regulation and a likely involvement in the modification of chromatin structure (Kortschak et al., 2000).
The ARID (A-T Rich Interaction Domain) is a helix-turn-helix motif-based DNA-binding domain, conserved in all eukaryotes
and diagnostic of a family that includes 15 distinct human proteins with important roles in development, tissue-specific
gene expression and proliferation control. Most ARID family members have not been characterized with respect to their
DNA-binding behavior, but it is already apparent that not all ARIDs conform to the pattern of binding AT-rich sequences
(Patsialou et al., 2005).
(taken from TOBFAC).
4 predicted putative ARID TF sequences;
blast HSP output, and multiple sequence alignment in
Soy - TFKB.
2 ARID sequences with annotations for soybean in PlantTFDB.
All are partial sequences.
This page was setup on May 23, 2009, last updated by Dr. Jeff Chen on June 6, 2009.