An efficient rapid system for assaying HBx-mediated transactivation

Zhou, Xiaoling; Shi, Haijun; Yang, Shaozhe; Sun, Pingnan

doi:10.1007/s10529-017-2334-1

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2018

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Cited by 2 publications

(1 citation statement)

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“…Time efficient and sensitive methods are essential in biotechnology in different areas as virology, cancer research or fermentation process (Wiegmann et al, 2018;Kang et al, 2018;Zhou et al, 2017) among others. Enzymatic activity measurements are essential in biotechnological process.…”

Section: Introductionmentioning

confidence: 99%

TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES

Martínez-Pérez¹,

Camacho-Ruiz²,

Estrada‐Alvarado³

et al. 2018

Rev.Mex.Ing.Quim.

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Section: Introductionmentioning

confidence: 99%

TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES

Martínez-Pérez¹,

Camacho-Ruiz²,

Estrada‐Alvarado³

et al. 2018

Rev.Mex.Ing.Quim.

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RBM24 stabilizes hepatitis B virus pregenomic RNA but inhibits core protein translation by targeting the terminal redundancy sequence

Yao

Yang

Huang

et al. 2018

Emerging Microbes & Infections

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The terminal redundancy (TR) sequence of the 3.5-kb hepatitis B virus (HBV) RNA contains sites that govern many crucial functions in the viral life cycle, including polyadenylation, translation, RNA packaging, and DNA synthesis. In the present study, RNA-binding motif protein 24 (RBM24) is shown to be involved in the modulation of HBV replication by targeting the TR of HBV RNA. In HBV-transfected hepatoma cell lines, both knockdown and overexpression of RBM24 led to decreased HBV replication and transcription. Ectopic expression of RBM24 inhibited HBV replication, which was partly restored by knockdown of RBM24, indicating that a proper level of RBM24 was required for HBV replication. The regulation of RBM24 of HBV replication and translation was achieved by the interaction between the RNA-binding domains of RBM24 and both the 5′ and 3′ TR of 3.5-kb RNA. RBM24 interacted with the 5′ TR of HBV pregenomic RNA (pgRNA) to block 80S ribosome assembly on HBV pgRNA and thus inhibited core protein translation, whereas the interaction between RBM24 and the 3′ TR enhanced the stability of HBV RNA. Finally, the regulatory function of RBM24 on HBV replication was further confirmed in a HBV infection model. In conclusion, the present study demonstrates the dual functions of RBM24 by interacting with different TRs of viral RNA and reveals that RBM24 is an important host gene for HBV replication.

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An efficient rapid system for assaying HBx-mediated transactivation

Abstract: Collectively, the GFP-based reporter system provides a rapid and accurate approach for analyzing transactivation ability of HBx.

Cited by 2 publications

References 32 publications

TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES

TIME-EFFICIENT pH-BASED METHOD TO QUANTIFY THE ACTIVITY OF ALKALINE AND HALO-ALKALINE PROTEASES

RBM24 stabilizes hepatitis B virus pregenomic RNA but inhibits core protein translation by targeting the terminal redundancy sequence

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