TY - JOUR
T1 - Crystallization and characterization of Smaug
T2 - A novel RNA-binding motif
AU - Green, Justin B.
AU - Edwards, Thomas A.
AU - Trincao, Jose
AU - Escalante, Carlos R.
AU - Wharton, Robin P.
AU - Aggarwal, Aneel K.
N1 - Funding Information:
We thank the staff at beamlines 19ID (APS) and X25 (BNL) for facilitating X-ray data collection and Alex Kentsis for assistance in the collection and analysis of the circular dichroism data. J.B.G. is supported by NIH Grant F32 GM20837, A.K.A. is supported by NIH Grant R01 GM62947, R.P.W is an Assistant Investigator of the HHMI, J.T. is supported by Praxis fellowship BD/13594/97 from Fundação para a Ciência e Tecnologia.
PY - 2002
Y1 - 2002
N2 - 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 = 129:3Å, c = 33:1Å, α = β = 90°, γ = 120° and diffract to 1.80 A° with synchrotron radiation. Initial characterization of this domain suggests that it encodes a novel RNA-binding motif.
AB - 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 = 129:3Å, c = 33:1Å, α = β = 90°, γ = 120° and diffract to 1.80 A° with synchrotron radiation. Initial characterization of this domain suggests that it encodes a novel RNA-binding motif.
UR - https://www.scopus.com/pages/publications/0036399160
U2 - 10.1016/S0006-291X(02)02327-6
DO - 10.1016/S0006-291X(02)02327-6
M3 - Article
C2 - 12372396
AN - SCOPUS:0036399160
SN - 0006-291X
VL - 297
SP - 1085
EP - 1088
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 5
ER -