» Articles » PMID: 25184952

Structures and Functions of Qβ Replicase: Translation Factors Beyond Protein Synthesis

Overview
Journal Int J Mol Sci
Publisher MDPI
Date 2014 Sep 4
PMID 25184952
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

Qβ replicase is a unique RNA polymerase complex, comprising Qβ virus-encoded RNA-dependent RNA polymerase (the catalytic β-subunit) and three host-derived factors: translational elongation factor (EF) -Tu, EF-Ts and ribosomal protein S1. For almost fifty years, since the isolation of Qβ replicase, there have been several unsolved, important questions about the mechanism of RNA polymerization by Qβ replicase. Especially, the detailed functions of the host factors, EF-Tu, EF-Ts, and S1, in Qβ replicase, which are all essential in the Escherichia coli (E. coli) host for protein synthesis, had remained enigmatic, due to the absence of structural information about Qβ replicase. In the last five years, the crystal structures of the core Qβ replicase, consisting of the β-subunit, EF-Tu and Ts, and those of the core Qβ replicase representing RNA polymerization, have been reported. Recently, the structure of Qβ replicase comprising the β-subunit, EF-Tu, EF-Ts and the N-terminal half of S1, which is capable of initiating Qβ RNA replication, has also been reported. In this review, based on the structures of Qβ replicase, we describe our current understanding of the alternative functions of the host translational elongation factors and ribosomal protein S1 in Qβ replicase as replication factors, beyond their established functions in protein synthesis.

Citing Articles

Removal of type IV pili by a small RNA virus.

Thongchol J, Yu Z, Harb L, Lin Y, Koch M, Theodore M Science. 2024; 384(6691):eadl0635.

PMID: 38574145 PMC: 11126211. DOI: 10.1126/science.adl0635.


Recent Advances in Structural Studies of Single-Stranded RNA Bacteriophages.

Thongchol J, Lill Z, Hoover Z, Zhang J Viruses. 2023; 15(10).

PMID: 37896763 PMC: 10610835. DOI: 10.3390/v15101985.


Mechanistic insights into tRNA cleavage by a contact-dependent growth inhibitor protein and translation factors.

Wang J, Yashiro Y, Sakaguchi Y, Suzuki T, Tomita K Nucleic Acids Res. 2022; 50(8):4713-4731.

PMID: 35411396 PMC: 9071432. DOI: 10.1093/nar/gkac228.


Protein unties the pseudoknot: S1-mediated unfolding of RNA higher order structure.

Lund P, Chatterjee S, Daher M, Walter N Nucleic Acids Res. 2019; 48(4):2107-2125.

PMID: 31832686 PMC: 7038950. DOI: 10.1093/nar/gkz1166.


Attenuation of Live-Attenuated Yellow Fever 17D Vaccine Virus Is Localized to a High-Fidelity Replication Complex.

Davis E, Beck A, Strother A, Thompson J, Widen S, Higgs S mBio. 2019; 10(5).

PMID: 31641088 PMC: 6805994. DOI: 10.1128/mBio.02294-19.


References
1.
Nissen P, Kjeldgaard M, Thirup S, Clark B, Nyborg J . The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold. Biochimie. 1996; 78(11-12):921-33. DOI: 10.1016/s0300-9084(97)86714-4. View

2.
Schuette J, Murphy 4th F, Kelley A, Weir J, Giesebrecht J, Connell S . GTPase activation of elongation factor EF-Tu by the ribosome during decoding. EMBO J. 2009; 28(6):755-65. PMC: 2666022. DOI: 10.1038/emboj.2009.26. View

3.
Karring H, Mathu S, van Duin J, Clark B, Kraal B, Knudsen C . Qbeta-phage resistance by deletion of the coiled-coil motif in elongation factor Ts. J Biol Chem. 2003; 279(3):1878-84. DOI: 10.1074/jbc.M306605200. View

4.
Osman T, Buck K . The tobacco mosaic virus RNA polymerase complex contains a plant protein related to the RNA-binding subunit of yeast eIF-3. J Virol. 1997; 71(8):6075-82. PMC: 191867. DOI: 10.1128/JVI.71.8.6075-6082.1997. View

5.
Haruna I, Spiegelman S . Specific template requirments of RNA replicases. Proc Natl Acad Sci U S A. 1965; 54(2):579-87. PMC: 219707. DOI: 10.1073/pnas.54.2.579. View