Identification of a matrix-associated region 5' of an immunoglobulin heavy chain variable region gene.

Webb, Carol F.; Das, Chhaya; Eneff, K.L.; Tucker, P W

doi:10.1128/mcb.11.10.5206

Cited by 59 publications

(63 citation statements)

References 25 publications

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“…Nuclear Matrix Isolation and MAR Binding Assay-Nuclei of the EL-4 T cell line were obtained by hypotonic lysis and purified by centrifugation through a cushion of 2 M sucrose, and nuclear matrices were isolated as described previously (1,8). Nuclear matrix binding was determined in an in vitro DNA-binding assay (8).…”

Section: Methodsmentioning

confidence: 99%

“…Nuclear matrix binding was determined in an in vitro DNA-binding assay (8). Briefly, plasmids containing the wild type or mutant L2a elements were linearized with NdeI and end-labeled with [␥-…”

Section: Methodsmentioning

confidence: 99%

“…The nuclear matrix is a proteinaceous subfraction that remains after extraction of nuclei with high salt concentrations, and it is thought to form a scaffold for chromosome attachment (3,4). MARs are typically 200 -300 bases in length, contain topoisomerase II cleavage sites, and occur on the average of one for every 30 kb of eukaryotic DNA (3,(5)(6)(7)(8). MARs have been increasingly observed near enhancer and promoter regions of genes (2, 8 -10), and the participation of MARs in regulating transcription of the immunoglobulin light chain (1) and heavy chain (11-13) genes has been described.…”

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confidence: 99%

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Interaction of the Nuclear Matrix-associated Region (MAR)-Binding Proteins, SATB1 and CDP/Cux, with a MAR Element (L2a) in an Upstream Regulatory Region of the Mouse CD8a Gene

Banan¹,

Rojas²,

Lee³

et al. 1997

Journal of Biological Chemistry

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Matrix-associated regions (MARs), AT-rich DNA segments that have an affinity for the nuclear matrix, have been shown to play a role in transcriptional regulation of eukaryotic genes. The present study demonstrates that a DNA element, called L2a, which has been implicated in the transcriptional regulation of the mouse CD8a gene encoding an important T cell coreceptor, is a MAR. Moreover, the identities of two nuclear proteins, L2a-P1 and L2a-P2, previously shown to bind to the L2a element, have been determined. The L2a-P1 protein found to be present in all CD8-positive T cell lines tested is SATB1, a known MAR-binding protein. The widely expressed L2a-P2 protein is CDP/Cux, a MAR-binding protein that has been associated with repression of gene transcription. Interaction of both proteins with the L2a element was studied using the missing nucleoside approach, DNase I footprinting, and electrophoretic mobility shift assays with wild type and mutant L2a elements. The data suggest that CDP/Cux bound to the L2a element is displaced by binding of SATB1 and the accompanying conformational change in the DNA lying between the primary binding sites of SATB1 and CDP/Cux. We suggest that displacement of CDP/Cux by SATB1 favors transcription of the CD8a gene, possibly by enhancing or altering its association with the nuclear matrix.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Interaction of the Nuclear Matrix-associated Region (MAR)-Binding Proteins, SATB1 and CDP/Cux, with a MAR Element (L2a) in an Upstream Regulatory Region of the Mouse CD8a Gene

Banan¹,

Rojas²,

Lee³

et al. 1997

Journal of Biological Chemistry

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“…Bright binds to AϩT-rich regions of the intronic heavy chain enhancer that have been identified as matrix association regions and regions 5Ј of some V H promoters, including the V1 S107 family gene (3,4). The cDNA for Bright was isolated in 1995, and the protein was shown to interact with DNA as a multimeric complex that includes multiple copies of Bright (4).…”

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confidence: 99%

Mutations in the DNA-binding Domain of the Transcription Factor Bright Act as Dominant Negative Proteins and Interfere with Immunoglobulin Transactivation

Nixon

Rajaiya

Webb

2004

Journal of Biological Chemistry

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The transcription factor Bright (or B cell regulator of IgH transcription) is a B cell-specific protein that was first discovered in a mature mouse B cell line, BCg3R1-d, as a mobilityshifted protein complex that caused 3-6-fold increases in heavy chain mRNA levels in response to stimulation with a T-dependent antigen and interleukin-5 (1, 2). Bright binds to AϩT-rich regions of the intronic heavy chain enhancer that have been identified as matrix association regions and regions 5Ј of some V H promoters, including the V1 S107 family gene (3, 4). The cDNA for Bright was isolated in 1995, and the protein was shown to interact with DNA as a multimeric complex that includes multiple copies of Bright (4).Recent studies suggest that Bruton's tyrosine kinase (〉tk), 1 the defective enzyme in xid (X-linked immunodeficiency disease) mice, is a component of the Bright DNA-binding complex (5). xid mice exhibit deficiencies in B cell development and abnormalities in immunoglobulin production (6, 7). Initial evidence indicated that the Bright DNA-binding complex was supershifted by antibodies that reacted with several different domains of Btk (5). Furthermore, Bright co-precipitated with Btk from wild type, activated splenic B cells, but Btk and Bright did not co-precipitate from xid B cells despite both proteins being present. These data suggested that Bright and Btk are functionally linked. However, the role of Bright in normal B cell development is unknown. Expression of Bright in both mouse and human tissues is tightly regulated at the level of transcription (8, 9). In the mouse, Bright mRNA was detected in all embryonic tissues, but became B-lymphocyte restricted in the adult. Bright mRNA is apparent at the pre-B and activated germinal center stages of B cell differentiation (8). The human Bright homologue (10) shows a similar expression pattern in the adult where mRNA expression is primarily limited to B lymphocytes of the pro-B cell, germinal center centroblasts, and mature recirculating subpopulations (9). Thus, in both the adult mouse and human, Bright expression is predominantly B cell-specific.Bright belongs to a growing family of proteins that bind DNA through an AϩT-rich interacting domain (ARID) (11). ARIDcontaining proteins are highly conserved throughout evolution where many of them play important roles as developmental regulators (11). ARID-containing proteins occur in all eukaryotic organisms and include 13 sequences in the human data base (11,12). Bright is the only member of the ARID family for which gene target sequences have been identified. One of the best characterized members of this family is the Dri (Drosophila homologue Dead Ringer) gene, first identified in 1996 (13). The ARID region of Dri is essential for anterior-posterior patterning and for muscle development in the fly embryo (14 -16). The crystal structure of the ARID region of Dri has been solved and revealed a unit of eight ␣-helices with a short two-stranded anti-parallel ␤-sheet (17). NMR analysis predicted that helices 5 and 6 together ...

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“…Interestingly MARs are also found near V H regions (Webb et al 1991;Goebel et al 2002), providing the possibility that they might help mediate juxtaposition of V H and D H J H gene segments to facilitate V H -D H J H rearrangement. Several proteins, including transcriptional activator Bright (Herrscher et al 1995) and the repressive cut-like protein Cux/CDP compete for binding in iEµ and V H MARs (Wang et al 1999;Goebel et al 2002).…”

Section: Cis-acting Elements In the Igh Locus And The Proteins That Bmentioning

confidence: 99%

YY1 helps to bring loose ends together: Figure 1.

Calame

Atchison²

2007

Genes Dev.

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Identification of a matrix-associated region 5' of an immunoglobulin heavy chain variable region gene.

Cited by 59 publications

References 25 publications

Interaction of the Nuclear Matrix-associated Region (MAR)-Binding Proteins, SATB1 and CDP/Cux, with a MAR Element (L2a) in an Upstream Regulatory Region of the Mouse CD8a Gene

Interaction of the Nuclear Matrix-associated Region (MAR)-Binding Proteins, SATB1 and CDP/Cux, with a MAR Element (L2a) in an Upstream Regulatory Region of the Mouse CD8a Gene

Mutations in the DNA-binding Domain of the Transcription Factor Bright Act as Dominant Negative Proteins and Interfere with Immunoglobulin Transactivation

YY1 helps to bring loose ends together: Figure 1.

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