CHARACTERIZATION OF PROTEINS BINDING TO ETS2 REGULATORY SEQUENCES
CHARACTERIZATION OF PROTEINS BINDING TO ETS2 REGULATORY SEQUENCES
批准号:
5201465
负责人:
J A LAUTENBERGER
金额:
$0.0万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至
中文摘要
ETS2启动子含有嘌呤/嘧啶链的延伸区
转录起始点上游的不对称(CT轨迹)。这个
这些序列的存在是完整表达ETS2所必需的。在…
CT轨迹中形成蛋白质复合体的至少两个区域
电泳迁移率改变分析(EMSA)已经被鉴定出来。这个
主要的复合体被发现与转录因子Sp1竞争良好
共识寡核苷酸。它还被发现与
纯Sp1蛋白复合体及其抗体的超移位
对抗Sp1。Sp1和核提取物表现出相似的DNaseI
示意图图案。
EMSA中与单链DNA形成的蛋白质-DNA复合体是
观察到的。它具有非常类似于的结合序列特异性
Pur-Alpha因子。然而,与之形成的络合物的流动性
核抽提物中的因子与重组的因子不同
Pur-Alpha。
英文摘要
The ETS2 promoter contains an extended region of purine/pyrimidine strand
asymmetry (CT track) upstream from the start site for transcription. The
presence of these sequences are required for full ETS2 expression. At
least two regions of the CT track that form protein complexes in the
electrophoretic mobility shift assay (EMSA) have been identified. The
major complex was found to compete well with a transcription factor Sp1
consensus oligonucleotide. It was also found to comigrate with the
protein complex of pure Sp1 and to supershift with antibodies raised
against Sp1. Both Sp1 and nuclear extracts exhibit similar DNaseI
footprint patterns.
A protein-DNA complex in the EMSA that forms with single-strand DNA was
observed. It has a binding sequence specificity that is very similar to
the Pur-alpha factor. However, the mobility of complexes that form with
the factor from nuclear extracts differs from that of recombinant
Pur-alpha.
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