Poly(A) tail recognition by a viral RNA element through assembly of a triple helix

Science

Volumn 330, Issue 6008, 2010, Pages 1244-1247

  Mitton Fry, Rachel M ^a   DeGregorio, Suzanne J ^a   Wang, Jimin ^b   Steitz, Thomas A ^b   Steitz, Joan A ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

POLYADENYLATED RNA; SMALL NUCLEOLAR RNA; VIRUS RNA;

ASSAY; CRYSTAL STRUCTURE; GENE EXPRESSION; GENETIC ANALYSIS; HYBRID; POLYPLOIDY; RESOLUTION; RNA;

ARTICLE; CRYSTAL STRUCTURE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; RNA HYBRIDIZATION; TRIPLE HELIX; VIRUS ASSEMBLY;

BASE PAIRING; CELL NUCLEUS; CRYSTALLOGRAPHY, X-RAY; HERPESVIRUS 8, HUMAN; MUTATION; NUCLEIC ACID CONFORMATION; POLY A; REGULATORY SEQUENCES, RIBONUCLEIC ACID; RIBOSWITCH; RNA STABILITY; RNA, MESSENGER; RNA, NUCLEAR; RNA, UNTRANSLATED; RNA, VIRAL;

HUMAN HERPESVIRUS 8;

EID: 78649422018     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1195858     Document Type: Article

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29. We thank S. Borah, K. Tycowski, K. Herbert, and K. Riley for critical reading of the manuscript and the entire Steitz laboratories for helpful discussion.We thank S. Strobel and G. Conn for the generous gifts of iridium(III) hexamine and 3′-hepatitis delta virus (HDV) plasmid, respectively. Special thanks to Y. Zuo and G. Blaha for crystallography assistance, P. Moore and E. Paulson for NMR assistance, and M.-D. Shu, D. Mishler, and K. Durniak for technical assistance. X-ray data were collected at the National Synchrotron Light Source (X29A) at Brookhaven National Laboratory (13). Financial support for this research was provided by NIH grant CA16038 to J.A.S. and NIH grant GM022778 to T.A.S. The content is solely the responsibility of the authors and does not necessarily represent the official views of NIH. R.M.M.-F. is supported by a Jane Coffin Childs Memorial Fund Postdoctoral fellowship. J.A.S. and T.A.S. are investigators of the Howard Hughes Medical Institute. Coordinates and structure factors have been deposited in the Protein Data Bank under accession code 3P22.