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Crystal structures and RNA-binding properties of Lsm proteins from archaea Sulfolobus acidocaldarius and Methanococcus vannielii: Similarity and difference of the U-binding mode.
Biochimie ( IF 3.9 ) Pub Date : 2020-05-15 , DOI: 10.1016/j.biochi.2020.05.001 N Lekontseva 1 , A Mikhailina 1 , M Fando 1 , O Kravchenko 1 , V Balobanov 1 , S Tishchenko 1 , A Nikulin 1
Biochimie ( IF 3.9 ) Pub Date : 2020-05-15 , DOI: 10.1016/j.biochi.2020.05.001 N Lekontseva 1 , A Mikhailina 1 , M Fando 1 , O Kravchenko 1 , V Balobanov 1 , S Tishchenko 1 , A Nikulin 1
Affiliation
Sm and Sm-like (Lsm) proteins are considered as an evolutionary conserved family involved in RNA metabolism in organisms from bacteria and archaea to human. Currently, the function of Sm-like archaeal proteins (SmAP) is not well understood. Here, we report the crystal structures of SmAP proteins from Sulfolobus acidocaldarius and Methanococcus vannielii and a comparative analysis of their RNA-binding sites. Our data show that these SmAPs have only a uridine-specific RNA-binding site, unlike their bacterial homolog Hfq, which has three different RNA-binding sites. Moreover, variations in the amino acid composition of the U-binding sites of the two SmAPs lead to a difference in protein affinity for oligo(U) RNA. Surface plasmon resonance data and nucleotide-binding analysis confirm the high affinity of SmAPs for uridine nucleotides and oligo(U) RNA and the reduced affinity for adenines, guanines, cytidines and corresponding oligo-RNAs. In addition, we demonstrate that MvaSmAP1 and SacSmAP2 are capable of melting an RNA hairpin and, apparently, promote its interaction with complementary RNA.
中文翻译:
来自古细菌Sulfolobus acidocaldarius和vanthanococcus vannielii的Lsm蛋白的晶体结构和RNA结合特性:U结合模式的异同。
Sm和Sm-like(Lsm)蛋白被认为是进化保守的家族,参与了从细菌,古细菌到人类等生物体的RNA代谢。目前,尚不完全了解Sm样古细菌蛋白(SmAP)的功能。在这里,我们报告了来自Sulfolobus acidocaldarius和Vanthanococcus vannielii的SmAP蛋白的晶体结构及其RNA结合位点的比较分析。我们的数据表明,这些SmAP仅具有尿苷特异性的RNA结合位点,与它们的细菌同源物Hfq不同,后者具有三个不同的RNA结合位点。此外,两个SmAP的U结合位点的氨基酸组成变化会导致蛋白质对oligo(U)RNA的亲和力不同。表面等离振子共振数据和核苷酸结合分析证实SmAPs对尿苷核苷酸和oligo(U)RNA的亲和力高,对腺嘌呤,鸟嘌呤,胞苷和相应的oligo-RNA的亲和力降低。此外,我们证明MvaSmAP1和SacSmAP2能够融化RNA发夹,并明显促进其与互补RNA的相互作用。
更新日期:2020-05-15
中文翻译:
来自古细菌Sulfolobus acidocaldarius和vanthanococcus vannielii的Lsm蛋白的晶体结构和RNA结合特性:U结合模式的异同。
Sm和Sm-like(Lsm)蛋白被认为是进化保守的家族,参与了从细菌,古细菌到人类等生物体的RNA代谢。目前,尚不完全了解Sm样古细菌蛋白(SmAP)的功能。在这里,我们报告了来自Sulfolobus acidocaldarius和Vanthanococcus vannielii的SmAP蛋白的晶体结构及其RNA结合位点的比较分析。我们的数据表明,这些SmAP仅具有尿苷特异性的RNA结合位点,与它们的细菌同源物Hfq不同,后者具有三个不同的RNA结合位点。此外,两个SmAP的U结合位点的氨基酸组成变化会导致蛋白质对oligo(U)RNA的亲和力不同。表面等离振子共振数据和核苷酸结合分析证实SmAPs对尿苷核苷酸和oligo(U)RNA的亲和力高,对腺嘌呤,鸟嘌呤,胞苷和相应的oligo-RNA的亲和力降低。此外,我们证明MvaSmAP1和SacSmAP2能够融化RNA发夹,并明显促进其与互补RNA的相互作用。