A phage RNA-binding protein binds to a non-cognate structured RNA and stabilizes its core structure.
Recent studies suggest that some RNA-binding proteins facilitate the folding of non-cognate RNAs. Here, we report that bacteriophage MS2 coat protein (MS2 CP) bound and promoted the catalytic activity of Candida group I ribozyme. Cloning of the MS2-bound RNA segments showed that this protein primarily interacts with the P5ab-P5 structure. Ultraviolet cross-linking and the T1 footprinting assay further showed that MS2 binding stabilized tertiary interactions, including the conserved L9-P5 interaction, and led to a more compact core structure. This mechanism is similar to that of the yeast mitochondrial tyrosyl-tRNA synthetase on other group I introns, suggesting that different RNA-binding proteins may use common mechanisms to support RNA structures.
Xie
Mao-Hua
MH
State Key Laboratory of Virology and Department of Biotechnology, College of Life Sciences, Wuhan University, Wuhan, Hubei 430072, China.
Wu
Qi-Jia
QJ
Jiang
Yan-Fei
YF
Bao
Penghui
P
Zhang
Yi
Y
D002175:Candida / Q000201:enzymology / Q000235:genetics; D036022:Capsid Proteins / Q000737:chemistry / Q000378:metabolism*; D017909:Levivirus / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D012331:RNA, Fungal / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D014466:Ultraviolet Rays
D036022:Capsid Proteins; D016337:RNA, Catalytic; D012331:RNA, Fungal; D016601:RNA-Binding Proteins