Crystallization and characterization of Smaug: a novel RNA-binding motif

被引:7
|
作者
Green, JB
Edwards, TA
Trincao, J
Escalante, CR
Wharton, RP
Aggarwal, AK
机构
[1] CUNY Mt Sinai Sch Med, Dept Physiol & Biophys, Struct Biol Program, New York, NY 10029 USA
[2] Duke Univ, Med Ctr, Howard Hughes Med Inst, Dept Genet, Durham, NC 27710 USA
关键词
D O I
10.1016/S0006-291X(02)02327-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 = 129.3 Angstrom, c = 33.1 Angstrom, alpha = beta = 90degrees, gamma = 120degrees and diffract to 1.80 Angstrom with synchrotron radiation. Initial characterization of this domain suggests that it encodes a novel RNA-binding motif.
引用
收藏
页码:1085 / 1088
页数:4
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