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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Ribosomal protein S18e as a putative molecular staple for the 18S rRNA 3'-major domain core.
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Ribosomal protein S18e as a putative molecular staple for the 18S rRNA 3'-major domain core.

机译：核糖体蛋白S18e作为18S rRNA 3'-主要结构域核心的假定分子主食。

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摘要

Ribosomal protein S18e is a structural constituent of the 40S ribosomal subunit. We obtained recombinant human ribosomal protein S18e and studied its structural and functional properties. With the use of CD spectroscopy we showed that the protein secondary structure is mainly helical and stable in the neutral pH range and at low urea concentrations. Applying multiple sequence alignment, we revealed that the protein structure has characteristics of the eukaryotic members of the ribosomal protein S13p family with additional extensions in the N-terminal and central parts that contain alpha-helices according to our prediction. S18e binds specifically and independently to an RNA transcript corresponding to the evolutionary core of the 3'-major domain of 18S rRNA. Hydroxyl radical footprinting showed that the binding site of S18e on the 18S rRNA is similar in general to the binding site of S13p on the 16S rRNA in the 30S ribosomal subunit, albeit the rRNA regions attributed to binding of the eukaryote-specific extensions of S18e were also detected. With magnesium ion concentration close to cellular conditions (2mM), protein binding caused substantial rearrangements in the rRNA transcript making it compact in such a manner that helices H29/H30 and H41-H43 form a bundle resembling their arrangement in the ribosome. Thus, S18e seems to act as a molecular staple fixing the 18S rRNA 3'-major domain core.
机译：核糖体蛋白S18e是40S核糖体亚基的结构成分。我们获得了重组人核糖体蛋白S18e，并研究了其结构和功能特性。通过使用CD光谱，我们证明了蛋白质二级结构在中性pH范围和低尿素浓度下主要呈螺旋状且稳定。应用多个序列比对，我们发现蛋白质结构具有核糖体蛋白S13p家族的真核成员特征，根据我们的预测，在包含α-螺旋的N末端和中央部分有额外的延伸。 S18e与独立于18S rRNA 3'-主要结构域进化核心的RNA转录物特异性结合。羟基自由基足迹显示，在18S rRNA上S18e的结合位点与在30S核糖体亚基中16S rRNA上的S13p的结合位点大致相似，尽管归因于S18e的真核生物特异性延伸的结合的rRNA区域是也被检测到。在镁离子浓度接近细胞条件（2mM）的情况下，蛋白质结合导致rRNA转录物中的大量重排，使其紧密排列，使得螺旋H29 / H30和H41-H43形成类似于核糖体中其排列的束。因此，S18e似乎起固定18S rRNA 3'-主要结构域核心的作用。

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