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多头绒泡菌端粒结合蛋白的特性分析

Characterization of a telomere-binding protein from Physarum polycephalum.

作者信息

Coren J S, Epstein E M, Vogt V M

机构信息

Section of Genetics and Development, Cornell University, Ithaca, New York 14853.

出版信息

Mol Cell Biol. 1991 Apr;11(4):2282-90. doi: 10.1128/mcb.11.4.2282-2290.1991.

DOI:10.1128/mcb.11.4.2282-2290.1991
PMID:2005910
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC359930/
Abstract

We have partially purified a nuclear protein (PPT) from Physarum polycephalum that binds to the extrachromosomal ribosomal DNA telomeres of this acellular slime mold. Binding is specific for the (T2AG3)n telomere repeats, as evidenced by nitrocellulose filter binding assays, by gel mobility shift assays with both DNA fragments and double-stranded oligonucleotides, and by DNase I footprinting. PPT is remarkably heat stable, showing undiminished binding activity after incubation at 90 degrees C. It sediments at 1.2S, corresponding to a molecular weight of about 10,000 (for a globular protein), and its binding activity is undiminished by incubation with RNase, suggesting that it is not a ribonucleoprotein. We hypothesize that PPT plays a structural role in telomeres, perhaps preventing nucleolytic degradation or promoting telomere extension by a telomere-specific terminal transferase.

摘要

我们已经从多头绒泡菌中部分纯化出一种核蛋白（PPT），该蛋白可与这种无细胞黏菌的染色体外核糖体DNA端粒结合。通过硝酸纤维素滤膜结合试验、DNA片段和双链寡核苷酸的凝胶迁移率变动分析以及DNase I足迹分析证明，这种结合对（T2AG3）n端粒重复序列具有特异性。PPT具有显著的热稳定性，在90℃孵育后仍保持未减弱的结合活性。它在1.2S处沉降，对应于约10,000的分子量（对于球状蛋白而言），并且其结合活性在与RNase孵育后未减弱，这表明它不是核糖核蛋白。我们推测PPT在端粒中起结构作用，可能是防止核酸酶降解或通过端粒特异性末端转移酶促进端粒延伸。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/e8f9d8da2eb9/molcellb00138-0524-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/bef5c5dd9772/molcellb00138-0520-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/390dc7becc8f/molcellb00138-0521-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/962c855e7bbd/molcellb00138-0521-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/cc6cd449e8bd/molcellb00138-0522-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/6d59eec80c03/molcellb00138-0523-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/a60198ad5c7f/molcellb00138-0523-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/e8f9d8da2eb9/molcellb00138-0524-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/bef5c5dd9772/molcellb00138-0520-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/390dc7becc8f/molcellb00138-0521-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/962c855e7bbd/molcellb00138-0521-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/cc6cd449e8bd/molcellb00138-0522-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/6d59eec80c03/molcellb00138-0523-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/a60198ad5c7f/molcellb00138-0523-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/57f0/359930/e8f9d8da2eb9/molcellb00138-0524-a.jpg

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本文引用的文献

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ORGANIC REQUIREMENTS AND SYNTHETIC MEDIA FOR GROWTH OF THE MYXOMYCETE PHYSARUM POLYCEPHALUM.多头绒泡菌生长所需的有机成分及合成培养基
J Bacteriol. 1963 Aug;86(2):324-31. doi: 10.1128/jb.86.2.324-331.1963.
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Protein tightly bound near the termini of the Physarum extrachromosomal rDNA palindrome.蛋白质紧密结合在多头绒泡菌染色体外rDNA回文序列的末端附近。
J Cell Biol. 1981 Oct;91(1):309-14. doi: 10.1083/jcb.91.1.309.
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Non-nucleosomal packaging of a tandemly repeated DNA sequence at termini of extrachromosomal DNA coding for rRNA in Tetrahymena.
一个编码端粒重复序列结合蛋白的酵母必需基因。
Mol Cell Biol. 1993 Feb;13(2):1306-14. doi: 10.1128/mcb.13.2.1306-1314.1993.
4
Identification and characterization of a putative telomere end-binding protein from Tetrahymena thermophila.嗜热四膜虫中一种假定的端粒末端结合蛋白的鉴定与表征
Mol Cell Biol. 1995 Mar;15(3):1144-53. doi: 10.1128/MCB.15.3.1144.
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ST-1, a 39-kilodalton protein in Trypanosoma brucei, exhibits a dual affinity for the duplex form of the 29-base-pair subtelomeric repeat and its C-rich strand.ST-1是布氏锥虫中的一种39千道尔顿的蛋白质，它对29个碱基对的亚端粒重复序列的双链形式及其富含C的链具有双重亲和力。
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Inaccessibility of the Euplotes telomere binding protein.真核草履虫端粒结合蛋白难以获取。
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Euplotes crassus has genes encoding telomere-binding proteins and telomere-binding protein homologs.厚甲游仆虫具有编码端粒结合蛋白和端粒结合蛋白同源物的基因。
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C-terminal truncation of RAP1 results in the deregulation of telomere size, stability, and function in Saccharomyces cerevisiae.RAP1的C末端截短导致酿酒酵母中端粒大小、稳定性和功能的失调。
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