Mechanism for Template-Independent Terminal Adenylation Activity of Qβ Replicase

被引:8
|
作者
Takeshita, Daijiro [1 ]
Yamashita, Seisuke [1 ]
Tomita, Kozo [1 ,2 ]
机构
[1] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, Tsukuba, Ibaraki 3058566, Japan
[2] Japan Sci & Technol Agcy JST, PRESTO, Kawaguchi, Saitama 3320012, Japan
关键词
DEPENDENT RNA-POLYMERASE; CCA-ADDING ENZYME; BACTERIOPHAGE QBETA REPLICASE; FACTORS EF-TU; MESSENGER-RNA; PROTEIN-BIOSYNTHESIS; POLY(A) POLYMERASE; STRUCTURAL BASIS; GENOMIC RNA; PHAGE RNA;
D O I
10.1016/j.str.2012.07.004
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
The genomic RNA of Q beta virus is replicated by Q beta replicase, a template-dependent RNA polymerase complex. Q beta replicase has an intrinsic template-independent RNA 3'-adenylation activity, which is required for efficient viral RNA amplification in the host cells. However, the mechanism of the template-independent 3'-adenylation of RNAs by Q beta replicase has remained elusive. We determined the structure of a complex that includes Q beta replicase, a template RNA, a growing RNA complementary to the template RNA, and ATP. The structure represents the terminal stage of RNA polymerization and reveals that the shape and size of the nucleotide-binding pocket becomes available for ATP accommodation after the nucleotide-binding template-dependent C-addition. The stacking interaction between the ATP and the neighboring Watson-Crick base pair, between the 5'-G in the template and the 3'-C in the growing RNA, contributes to the nucleotide specificity. Thus, the template for the template-independent 3'-adenylation by Q beta replicase is the RNA and protein ribonucleoprotein complex.
引用
收藏
页码:1661 / 1669
页数:9
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