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通过荧光偏振研究大肠杆菌核糖体蛋白S1的片段灵活性。

Segmental flexibility in Escherichia coli ribosomal protein S1 as studied by fluorescence polarization.

作者信息

Chu Y G, Cantor C R

出版信息

Nucleic Acids Res. 1979;6(6):2363-79. doi: 10.1093/nar/6.6.2363.

DOI:10.1093/nar/6.6.2363
PMID:379818
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC327856/
Abstract

Ribosomal protein S1 covalently reacts with approximately one equivalent of iodoacetylethylenediamine (1,5-napthol sulfonate (IAEDANS) or iodoacetylaminofluorescein (IAAF). The product AEDANS-S1 can bind to 30S ribosomal subunits lacking S1 as shown by polyacrylamide-agarose gel electrophoresis AEDANS-S1 and AAF-S1 when added back to S1-depleted 30S subunits modulate poly(U)-dependent polyphenylalanine synthesis in the presence of IF3 in a very similar way to unmodified S1. AEDANS-S1 also stimulates RI7-dependent fMet-tRNA binding to 1.0M NH4C1 washed ribosomes whereas AAF-S1 does not. Both static and nanosecond fluorescence polarization techniques were used to study the rotational motions of AEDANS-S1. Several previous studies had indicated that S1 is a highly extended protein which can be modeled by a prolate ellipsoid with an axial ratio of 10 to 1. However, the rotational correlation time we find is about half that expected for such a particle. This suggests that S1 is a flexible protein with at least two domains that can rotate independently.

摘要

核糖体蛋白S1与大约一当量的碘乙酰乙二胺（1,5-萘酚磺酸盐（IAEDANS）或碘乙酰氨基荧光素（IAAF））发生共价反应。如聚丙烯酰胺-琼脂糖凝胶电泳所示，产物AEDANS-S1可与缺乏S1的30S核糖体亚基结合。当将AEDANS-S1和AAF-S1重新添加到缺乏S1的30S亚基中时，在IF3存在的情况下，它们以与未修饰的S1非常相似的方式调节聚（U）依赖性聚苯丙氨酸的合成。AEDANS-S1还刺激RI7依赖性fMet-tRNA与1.0M NH4C1洗涤过的核糖体结合，而AAF-S1则不能。静态和纳秒荧光偏振技术均用于研究AEDANS-S1的旋转运动。先前的几项研究表明，S1是一种高度伸展的蛋白质，可以用轴比为10比1的长椭球体来建模。然而，我们发现的旋转相关时间约为此类粒子预期时间的一半。这表明S1是一种具有至少两个可独立旋转结构域的柔性蛋白质。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73f7/327856/5f0c6cd05be1/nar00447-0329-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73f7/327856/cebd95399ffd/nar00447-0327-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73f7/327856/5f0c6cd05be1/nar00447-0329-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73f7/327856/cebd95399ffd/nar00447-0327-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/73f7/327856/5f0c6cd05be1/nar00447-0329-a.jpg

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Structural basis for the interaction of protein S1 with the Escherichia coli ribosome.蛋白质S1与大肠杆菌核糖体相互作用的结构基础。

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