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甲状腺激素受体的单体、同二聚体及可能的异二聚体形式的差异性DNA结合

Differential DNA binding by monomeric, homodimeric, and potentially heteromeric forms of the thyroid hormone receptor.

作者信息

Lazar M A, Berrodin T J, Harding H P

机构信息

Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104.

出版信息

Mol Cell Biol. 1991 Oct;11(10):5005-15. doi: 10.1128/mcb.11.10.5005-5015.1991.

DOI:10.1128/mcb.11.10.5005-5015.1991
PMID:1922030
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC361489/
Abstract

Binding of the thyroid hormone receptor (TR) to thyroid hormone-responsive elements (TREs) is crucial for regulation of gene expression by thyroid hormone. The TR binds to each half-site of a palindromic TRE separately, as a monomer, or simultaneously, as a homodimer. In addition, the TR monomer interacts with a 42-kDa protein that may be responsible for an increase in the apparent size and stability of the TR-TRE complex after incubation with liver nuclear extract. The multiple DNA-binding forms of the TR contact the TRE differently but compete for binding in a dynamic equilibrium which is highly dependent on the relative concentrations of TR and nuclear protein. Thus, protein-protein interactions are likely to determine the context in which the TR binds to target genes and regulates the transcriptional response to thyroid hormone.

摘要

甲状腺激素受体(TR)与甲状腺激素反应元件(TREs)的结合对于甲状腺激素调节基因表达至关重要。TR作为单体分别与回文TRE的每个半位点结合,或作为同二聚体同时结合。此外,TR单体与一种42 kDa的蛋白质相互作用,该蛋白质可能是导致与肝核提取物孵育后TR-TRE复合物表观大小和稳定性增加的原因。TR的多种DNA结合形式与TRE的接触方式不同,但在高度依赖于TR和核蛋白相对浓度的动态平衡中竞争结合。因此,蛋白质-蛋白质相互作用可能决定TR与靶基因结合并调节对甲状腺激素转录反应的环境。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/1aefbcb77258/molcellb00034-0218-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/d1ee6f33f8e3/molcellb00034-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/f6ae2b8e4346/molcellb00034-0214-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/d4b3c6023edb/molcellb00034-0214-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/1e7d30d92f23/molcellb00034-0215-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/decae61936a0/molcellb00034-0216-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/642ce9fb740e/molcellb00034-0217-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/4d9e42cdcd77/molcellb00034-0217-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/1aefbcb77258/molcellb00034-0218-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/d1ee6f33f8e3/molcellb00034-0213-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/f6ae2b8e4346/molcellb00034-0214-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/d4b3c6023edb/molcellb00034-0214-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/1e7d30d92f23/molcellb00034-0215-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/decae61936a0/molcellb00034-0216-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/642ce9fb740e/molcellb00034-0217-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/4d9e42cdcd77/molcellb00034-0217-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b5c/361489/1aefbcb77258/molcellb00034-0218-a.jpg

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