Green Justin B, Edwards Thomas A, Trincao Jose, Escalante Carlos R, Wharton Robin P, Aggarwal Aneel K
Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.
Biochem Biophys Res Commun. 2002 Oct 11;297(5):1085-8. doi: 10.1016/s0006-291x(02)02327-6.
During Drosophila embryogenesis, Smaug protein represses translation of Nanos through an interaction with a specific element in its 3(')UTR. The repression occurs in the bulk cytoplasm of the embryo; Nanos is, however, successfully translated in the specialized cytoplasm of the posterior pole. This generates a gradient of Nanos emanating from the posterior pole that is essential for organizing proper abdominal segmentation. To understand the structural basis of RNA binding and translational control, we have crystallized a domain of Drosophila Smaug that binds RNA. The crystals belong to the space group R3 with unit cell dimensions of a=b=129.3A, c=33.1A, alpha=beta=90 degrees, gamma=120 degrees and diffract to 1.80A with synchrotron radiation. Initial characterization of this domain suggests that it encodes a novel RNA-binding motif.
在果蝇胚胎发育过程中，Smaug蛋白通过与Nanos 3(')UTR中的特定元件相互作用来抑制其翻译。这种抑制发生在胚胎的大量细胞质中；然而，Nanos在后极的特化细胞质中成功翻译。这在后极产生了一个Nanos梯度，这对于正确组织腹部节段至关重要。为了理解RNA结合和翻译控制的结构基础，我们结晶了果蝇Smaug中与RNA结合的一个结构域。这些晶体属于空间群R3，晶胞参数为a = b = 129.3埃，c = 33.1埃，α = β = 90度，γ = 120度，在同步辐射下衍射至1.80埃。对该结构域的初步表征表明它编码一种新的RNA结合基序。
