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一种与小麦亮氨酸拉链蛋白相似的拟南芥G盒结合蛋白,被鉴定为HBP-1。

An Arabidopsis thaliana G-box-binding protein similar to the wheat leucine zipper protein identified as HBP-1.

作者信息

Schindler U, Ecker J R, Cashmore A R

机构信息

Department of Biology, University of Pennsylvania, Philadelphia 19104.

出版信息

Symp Soc Exp Biol. 1991;45:211-8.

PMID:1843410
Abstract

G-box (CCACGTGG) like sequences are present in a variety of plant promoters and in many cases they have been demonstrated to be required for maximal expression of the corresponding gene. A nuclear protein, GBF, interacts specifically with the G-box motif of several RBCS and CAB promoters. Here we describe the isolation of a cDNA from Arabidopsis thaliana that encodes a protein, designated GBF-1, with DNA binding properties similar to GBF. GBF-1 is characterized by a basic/leucine zipper motif which is strikingly similar to the wheat protein identified as HBP-1. GBF-1 also interacts with an oligonucleotide derived from the wheat histone 3 promoter containing the binding site (hexamer, TGACGT) for HBP-1. This DNA element also contains a G-box-like motif, modification of which results in loss in binding of GBF-1.

摘要

类G盒(CCACGTGG)序列存在于多种植物启动子中,并且在许多情况下,已证明它们是相应基因最大程度表达所必需的。一种核蛋白GBF能与几种RBCS和CAB启动子的G盒基序特异性相互作用。在此,我们描述了从拟南芥中分离出一个cDNA,它编码一种名为GBF-1的蛋白质,其具有与GBF相似的DNA结合特性。GBF-1的特征是具有一个碱性/亮氨酸拉链基序,该基序与被鉴定为HBP-1的小麦蛋白极为相似。GBF-1还与来自小麦组蛋白3启动子的寡核苷酸相互作用,该寡核苷酸含有HBP-1的结合位点(六聚体,TGACGT)。这个DNA元件也包含一个类G盒基序,对其进行修饰会导致GBF-1结合能力丧失。

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