Structural basis of RNA binding discrimination between bacteriophages Qβ and MS2

被引:29
作者
Horn, WT
Tars, K
Grahn, E
Heigstrand, C
Baron, AJ
Lago, H
Adams, CJ
Peabody, DS
Phillips, SEV
Stonehouse, NJ
Liljas, L
Stockley, PG [1 ]
机构
[1] Univ Leeds, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England
[2] Uppsala Univ, Dept Cell & Mol Biol, SE-75124 Uppsala, Sweden
[3] Univ New Mexico, Dept Mol Genet & Microbiol, Albuquerque, NM 87131 USA
[4] Univ New Mexico, Canc Res & Treatment Ctr, Albuquerque, NM 87131 USA
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
D O I
10.1016/j.str.2005.12.006
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
Sequence-specific interactions between RNA stemloops and coat protein (CP) subunits play vital roles in the life cycles of the RNA bacteriophages, e.g., by allowing translational repression of their replicase cistrons and tagging their own RNA genomes for encapsidation. The Cps of bacteriophages Q beta and MS2 each discriminate in favor of their cognate translational operators, even in the presence of closely related operators from other phages in vivo. Discrete mutations within the MS2 CP have been shown to relax this discrimination in vitro. We have determined the structures of eight complexes between such mutants and both MS2 and GO stem-loops with X-ray crystallography. In conjunction with previously determined in vivo repression data, the structures enable us to propose the molecular basis for the discrimination mechanism.
引用
收藏
页码:487 / 495
页数:9
相关论文
共 36 条
[1]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[2]  
Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254
[3]   Crystal structure of an RNA aptamer protein complex at 2.8 Å resolution [J].
Convery, MA ;
Rowsell, S ;
Stonehouse, NJ ;
Ellington, AD ;
Hirao, I ;
Murray, JB ;
Peabody, DS ;
Phillips, SEV ;
Stockley, PG .
NATURE STRUCTURAL BIOLOGY, 1998, 5 (02) :133-139
[4]  
Delano WL., 2002, The PyMOL Molecular Graphics System
[5]   ACCURATE BOND AND ANGLE PARAMETERS FOR X-RAY PROTEIN-STRUCTURE REFINEMENT [J].
ENGH, RA ;
HUBER, R .
ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :392-400
[6]   The crystal structure of bacteriophage Q beta at 3.5 angstrom resolution [J].
Golmohammadi, R ;
Fridborg, K ;
Bundule, M ;
Valegard, K ;
Liljas, L .
STRUCTURE, 1996, 4 (05) :543-554
[7]   THE REFINED STRUCTURE OF BACTERIOPHAGE-MS2 AT 2-CENTER-DOT-8-ANGSTROM RESOLUTION [J].
GOLMOHAMMADI, R ;
VALEGARD, K ;
FRIDBORG, K ;
LILJAS, L .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 234 (03) :620-639
[8]   Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids:: Implications for binding requirements [J].
Grahn, E ;
Stonehouse, NJ ;
Murray, JB ;
Van den Worm, S ;
Valegård, K ;
Fridborg, K ;
Stockley, PG ;
Liljas, L .
RNA, 1999, 5 (01) :131-138
[9]  
Grahn E, 2001, RNA, V7, P1616
[10]   Deletion of a single hydrogen bonding atom from the MS2 RNA operator leads to dramatic rearrangements at the RNA-coat protein interface [J].
Grahn, E ;
Stonehouse, NJ ;
Adams, CJ ;
Fridborg, K ;
Beigelman, L ;
Matulic-Adamic, J ;
Warriner, SL ;
Stockley, PG ;
Liljas, L .
NUCLEIC ACIDS RESEARCH, 2000, 28 (23) :4611-4616