Cloning, expression, purification and preliminary crystallographic studies of the adenylate/uridylate-rich element-binding protein HuR complexed with its target RNA.
Adenylate/uridylate-rich elements (AREs), which are found in the 3'-untranslated region (UTR) of many mRNAs, influence the stability of cytoplasmic mRNA. HuR (human antigen R) binds to AREs and regulates various genes. In order to reveal the RNA-recognition mechanism of HuR protein, an RNA-binding region of human HuR containing two N-terminal RNA-recognition motif domains bound to an 11-base RNA fragment has been crystallized. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.4, b = 44.9, c = 91.1 A. X-ray diffraction data were collected to 1.8 A resolution.
Iyaguchi
Daisuke
D
Health Sciences University of Hokkaido, Japan.
Yao
Min
M
Tanaka
Isao
I
Toyota
Eiko
E
D000954:Antigens, Surface / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D051959:ELAV Proteins; D000067780:ELAV-Like Protein 1; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D038621:Regulatory Sequences, Ribonucleic Acid / Q000235:genetics*
D000954:Antigens, Surface; D051959:ELAV Proteins; D000067780:ELAV-Like Protein 1; C098770:ELAVL1 protein, human; D016601:RNA-Binding Proteins; D038621:Regulatory Sequences, Ribonucleic Acid; D012313:RNA