Ig S gamma-specific DNA binding protein SNAP is related to the helix-loop-helix transcription factor E47.

Ig S gamma-specific DNA binding protein SNAP is related to the helix-loop-helix transcription factor E47.
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Ig S γ 特异性 DNA 结合蛋白 SNAP 与螺旋-环-螺旋转录因子 E47 相关。

DOI:
10.1093/intimm/9.7.1021
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发表时间:
1997
影响因子:
4.4
通讯作者:
Kenter,AL
Kenter,AL
中科院分区:
医学3区
文献类型:
--
作者:
Ma,L;Hu,B;Kenter,AL

文献摘要

被引文献

相似文献

SNAP是一种DNA结合蛋白,对S γ开关区域具有特异性。两个E-2盒共有结合基序位于SNAP识别位点内。直接和竞争结合分析表明,截短形式的E47转录因子,E47 S,是能够与SNAP结合基序的特异性相互作用。Pl.S γ 3.A.1探针上E47 S结合的甲基化干扰模式与先前获得的SNAP结合活性的甲基化干扰模式相似,并且也与microE 5探针上E47 S的甲基化干扰模式相关。纯化的E47 S与SNAP识别基序的相互作用是合作的,并形成复合物,其迁移速度比E47 S同源二聚体复合物慢。SNAP与在BCF-1中发现的全长E47同源二聚体的区别在于其在凝胶迁移试验中的迁移位置、竞争结合结果的差异及其与抗E47抗体的独特反应性。SNAP与E47相关,这是通过S γ 3 A位点DNA上类似的甲基化干扰模式及其与抗E47 mAb的反应性来判断的。抗E47抗体阻断SNAP与其同源位点的结合,而抗E47抗体超转移与microE 5识别位点结合的E47同二聚体。因此,SNAP可能是含有E47或高度相关蛋白质的异源寡聚物种类。
SNAP, a DNA-binding protein, is specific for the S gamma switch regions. Two E-2 box consensus binding motifs are located within the SNAP recognition site. Direct- and competition-binding analyses demonstrate that a truncated form of the E47 transcription factor, E47S, is capable of specific interactions with the SNAP binding motif. The methylation interference pattern for E47S binding on the pl.S gamma 3.A.1 probe was similar to that previously obtained for SNAP binding activity and was also related to that found for E47S on the microE5 probe. The interaction of purified E47S with the SNAP recognition motif was cooperative and formed complexes which migrated more slowly than the E47S homodimer complex. SNAP is distinguished from full-length E47 homodimers, found in BCF-1, by its migration position in the gel shift assay, differences in the competition-binding results and its unique reactivity with anti-E47 antibodies. SNAP is related to E47 as judged by a similar methylation interference pattern on S gamma 3 A site DNA and by its reactivity with anti-E47 mAb. The anti-E47 antibodies block SNAP binding to its cognate site, whereas anti-E47 antibodies supershift E47 homodimers bound to the microE5 recognition site. Thus, SNAP may be a hetero-oligomeric species containing E47 or highly related proteins.