scholarly journals Derepression of MicroRNA-mediated Protein Translation Inhibition by Apolipoprotein B mRNA-editing Enzyme Catalytic Polypeptide-like 3G (APOBEC3G) and Its Family Members

2007 ◽  
Vol 282 (46) ◽  
pp. 33632-33640 ◽  
Author(s):  
Jialing Huang ◽  
Zhihui Liang ◽  
Bin Yang ◽  
Heng Tian ◽  
Jin Ma ◽  
...  
Keyword(s):  
Reporter Gene ◽  
Apolipoprotein B ◽  
Cytidine Deaminase ◽  
Family Members ◽  
Cellular Function ◽  
Luciferase Reporter ◽  
Mrna Editing ◽  
Processing Bodies ◽  
Cytidine Deaminase Activity ◽  
Editing Enzyme

The apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G or A3G) and its fellow cytidine deaminase family members are potent restrictive factors for human immunodeficiency virus type 1 (HIV-1) and many other retroviruses. A3G interacts with a vast spectrum of RNA-binding proteins and is located in processing bodies and stress granules. However, its cellular function remains to be further clarified. Using a luciferase reporter gene and green fluorescent protein reporter gene, we demonstrate that A3G and other APOBEC family members can counteract the inhibition of protein synthesis by various microRNAs (miRNAs) such as mir-10b, mir-16, mir-25, and let-7a. A3G could also enhance the expression level of miRNA-targeted mRNA. Further, A3G facilitated the association of microRNA-targeted mRNA with polysomes rather than with processing bodies. Intriguingly, experiments with a C288A/C291A A3G mutant indicated that this function of A3G is separable from its cytidine deaminase activity. Our findings suggest that the major cellular function of A3G, in addition to inhibiting the mobility of retrotransposons and replication of endogenous retroviruses, is most likely to prevent the decay of miRNA-targeted mRNA in processing bodies.

scholarly journals The p27 catalytic subunit of the apolipoprotein B mRNA editing enzyme is a cytidine deaminase.

1993 ◽  
Vol 268 (28) ◽  
pp. 20709-20712 ◽  
Author(s):  
N Navaratnam ◽  
J.R. Morrison ◽  
S Bhattacharya ◽  
D Patel ◽  
T Funahashi ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Cytidine Deaminase ◽  
Catalytic Subunit ◽  
Mrna Editing ◽  
Editing Enzyme

scholarly journals Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1): structure–function relationships of RNA editing and dimerization

1999 ◽  
Vol 40 (4) ◽  
pp. 623-635 ◽  
Author(s):  
Ba-Bie Teng ◽  
Scott Ochsner ◽  
Qian Zhang ◽  
Kizhake V. Soman ◽  
Paul P. Lau ◽  
...  
Keyword(s):  
Structure Function ◽  
Rna Editing ◽  
Apolipoprotein B ◽  
Mutational Analysis ◽  
Mrna Editing ◽  
Editing Enzyme

scholarly journals Optimization of the apolipoprotein B mRNA editing enzyme catalytic polypeptidelike-3G (APOBEC3G) gene to enhance its expression in Escherichia coli

2020 ◽  
Vol 29 (2) ◽  
pp. 120-8
Author(s):  
Rizkyana Avissa ◽  
Silvia Tri Widyaningtyas ◽  
Budiman Bela
Keyword(s):  
Escherichia Coli ◽  
Apolipoprotein B ◽  
Plasmid Vector ◽  
Nitrilotriacetic Acid ◽  
Mrna Editing ◽  
Specific Domain ◽  
Iptg Induction ◽  
E Coli ◽  
Gene Coding ◽  
Editing Enzyme

BACKGROUND Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like-3G (APOBEC3G) can abolish HIV infection by inducing lethal mutations in the HIV genome. The HIV protein virion infectivity factor (Vif) can interact with APOBEC3G protein and cause its degradation. Development of a method that can screen substances inhibiting the APOBEC3G-Vif interaction is necessary for identification of substances that potentially used in anti-HIV drug development. In order to increase expression of recombinant APOBEC3G protein that will be used in APOBEC3G-Vif interaction assay, we developed an optimized APOBEC3G gene for expression in Escherichia coli.  METHODS The gene coding APOBEC3G was codon-optimized in accordance with prokaryotic codon using DNA 2.0 software to avoid bias codons that could inhibit its expression. The APOBEC3G gene was synthesized and sub-cloned into pQE80L plasmid vector. pQE80L containing APOBEC3G was screened by polymerase chain reaction, enzyme restriction, and sequencing to verify its DNA sequence. The recombinant APOBEC3G was expressed in E. coli under isopropyl-β-D-thiogalactoside (IPTG) induction and purified by using nickel-nitrilotriacetic acid (Ni-NTA) resin.  RESULTS The synthetic gene coding APOBEC3G was successfully cloned into the pQE80L vector and could be expressed abundantly in E. coli BL21 in the presence of IPTG.  CONCLUSIONS Recombinant APOBEC3G is robustly expressed in E. coli BL21, and the APOBEC3G protein could be purified by using Ni-NTA. The molecular weight of the recombinant APOBEC3G produced is smaller than the expected value. However, the protein is predicted to be able to interact with Vif because this interaction is determined by a specific domain located on the N-terminal of APOBEC3G. 

scholarly journals Purification and Molecular Cloning of a Novel Essential Component of the Apolipoprotein B mRNA Editing Enzyme-Complex

2000 ◽  
Vol 275 (26) ◽  
pp. 19848-19856 ◽  
Author(s):  
Heinrich Lellek ◽  
Romy Kirsten ◽  
Ines Diehl ◽  
Frank Apostel ◽  
Friedrich Buck ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Apolipoprotein B ◽  
Enzyme Complex ◽  
Mrna Editing ◽  
Essential Component ◽  
Editing Enzyme

scholarly journals Apolipoprotein B mRNA–Editing Enzyme, Catalytic Polypeptide–Like 3G: A Possible Role in the Resistance to HIV of HIV‐Exposed Seronegative Individuals

2007 ◽  
Vol 195 (7) ◽  
pp. 960-964 ◽  
Author(s):  
Mara Biasin ◽  
Luca Piacentini ◽  
Sergio Lo Caputo ◽  
Yasuyoshi Kanari ◽  
Giuliana Magri ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Mrna Editing ◽  
Hiv Exposed ◽  
Editing Enzyme

Assignment of the Gene Encoding the Human Apolipoprotein B mRNA Editing Enzyme (APOBEC1) to Chromosome 12p13.1

Genomics ◽  
1994 ◽  
Vol 24 (2) ◽  
pp. 414-415 ◽  
Author(s):  
Rafael Espinosa ◽  
Toru Funahashi ◽  
Christos Hadjiagapiou ◽  
Michelle M. Le Beau ◽  
Nicholas O. Davidson
Keyword(s):  
Apolipoprotein B ◽  
Mrna Editing ◽  
Gene Encoding ◽  
Human Apolipoprotein ◽  
Editing Enzyme
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