Altered‐specificity mutants of the HIV Rev arginine‐rich motif‐RRE IIB interaction

2020 ◽  
Vol 33 (6) ◽  
Author(s):  
Nicole G. Raad ◽  
Ingrid R. Ghattas ◽  
Ryo Amano ◽  
Natsuki Watanabe ◽  
Taiichi Sakamoto ◽  
...  
Keyword(s):  
Arginine Rich Motif

SRP RNA Remodeling by SRP68 Explains Its Role in Protein Translocation

Science ◽  
2014 ◽  
Vol 344 (6179) ◽  
pp. 101-104 ◽  
Author(s):  
Jan Timo Grotwinkel ◽  
Klemens Wild ◽  
Bernd Segnitz ◽  
Irmgard Sinning
Keyword(s):  
Ribosomal Rna ◽  
Protein Targeting ◽  
Rna Binding ◽  
Protein Translocation ◽  
Signal Recognition Particle ◽  
Structural Basis ◽  
Signal Recognition ◽  
Rna Remodeling ◽  
Srp Rna ◽  
Arginine Rich Motif

The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19. SRP68-RBD is a tetratricopeptide-like module that binds to a RNA three-way junction, bends the RNA, and inserts an α-helical arginine-rich motif (ARM) into the major groove. The ARM opens the conserved 5f RNA loop, which in ribosome-bound SRP establishes a contact to ribosomal RNA. Our data provide the structural basis for eukaryote-specific, SRP68-driven RNA remodeling required for protein translocation.

scholarly journals Roles of the AX4GKS and Arginine-Rich Motifs of Hepatitis C Virus RNA Helicase in ATP- and Viral RNA-Binding Activity

2000 ◽  
Vol 74 (20) ◽  
pp. 9732-9737 ◽  
Author(s):  
Shin C. Chang ◽  
Ju-Chien Cheng ◽  
Yi-Hen Kou ◽  
Chuan-Hong Kao ◽  
Chiung-Hui Chiu ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Rna Binding ◽  
Atp Hydrolysis ◽  
Nonstructural Protein ◽  
Binding Activity ◽  
Viral Rna ◽  
Atp Binding ◽  
Rna Unwinding ◽  
Arginine Rich Motif

ABSTRACT The nonstructural protein 3 (NS3) of hepatitis C virus (HCV) possesses protease, nucleoside triphosphatase, and helicase activities. Although the enzymatic activities have been extensively studied, the ATP- and RNA-binding domains of the NS3 helicase are not well-characterized. In this study, NS3 proteins with point mutations in the conserved helicase motifs were expressed inEscherichia coli, purified, and analyzed for their effects on ATP binding, RNA binding, ATP hydrolysis, and RNA unwinding. UV cross-linking experiments indicate that the lysine residue in the AX4GKS motif is directly involved in ATP binding, whereas the NS3(GR1490DT) mutant in which the arginine-rich motif (1486-QRRGRTGR-1493) was changed to QRRDTTGR bound ATP as well as the wild type. The binding activity of HCV NS3 helicase to the viral RNA was drastically reduced with the mutation at Arg1488 (R1488A) and was also affected by the K1236E substitution in the AX4GKS motif and the R1490A and GR1490DT mutations in the arginine-rich motif. Previously, Arg1490 was suggested, based on the crystal structure of an NS3-deoxyuridine octamer complex, to directly interact with the γ-phosphate group of ATP. Nevertheless, our functional analysis demonstrated the critical roles of Arg1490 in binding to the viral RNA, ATP hydrolysis, and RNA unwinding, but not in ATP binding.

scholarly journals Oligomers of the Arginine-rich Motif of the HIV-1 TAT Protein Are Capable of Transferring Plasmid DNA into Cells

2003 ◽  
Vol 278 (13) ◽  
pp. 11411-11418 ◽  
Author(s):  
Carsten Rudolph ◽  
Christian Plank ◽  
James Lausier ◽  
Ulrike Schillinger ◽  
Rainer H. Müller ◽  
...  
Keyword(s):  
Plasmid Dna ◽  
Tat Protein ◽  
Hiv 1 ◽  
Arginine Rich Motif

scholarly journals Insights into HIV-1 proviral transcription from integrative structure and dynamics of the Tat:AFF4:P-TEFb:TAR complex

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Ursula Schulze-Gahmen ◽  
Ignacia Echeverria ◽  
Goran Stjepanovic ◽  
Yun Bai ◽  
Huasong Lu ◽  
...  
Keyword(s):  
Major Groove ◽  
Binding Model ◽  
Saxs Data ◽  
Recognition Motif ◽  
Structure And Dynamics ◽  
Hydrogen Deuterium ◽  
Central Loop ◽  
Binding Loop ◽  
Hiv 1 ◽  
Arginine Rich Motif

HIV-1 Tat hijacks the human superelongation complex (SEC) to promote proviral transcription. Here we report the 5.9 Å structure of HIV-1 TAR in complex with HIV-1 Tat and human AFF4, CDK9, and CycT1. The TAR central loop contacts the CycT1 Tat-TAR recognition motif (TRM) and the second Tat Zn2+-binding loop. Hydrogen-deuterium exchange (HDX) shows that AFF4 helix 2 is stabilized in the TAR complex despite not touching the RNA, explaining how it enhances TAR binding to the SEC 50-fold. RNA SHAPE and SAXS data were used to help model the extended (Tat Arginine-Rich Motif) ARM, which enters the TAR major groove between the bulge and the central loop. The structure and functional assays collectively support an integrative structure and a bipartite binding model, wherein the TAR central loop engages the CycT1 TRM and compact core of Tat, while the TAR major groove interacts with the extended Tat ARM.

Tuning the Transport Properties of HIV-1 Tat Arginine-Rich Motif in Living Cells

Traffic ◽  
2008 ◽  
Vol 9 (4) ◽  
pp. 528-539 ◽  
Author(s):  
Francesco Cardarelli ◽  
Michela Serresi ◽  
Ranieri Bizzarri ◽  
Fabio Beltram
Keyword(s):  
Transport Properties ◽  
Living Cells ◽  
Hiv 1 ◽  
Arginine Rich Motif

scholarly journals Functional Replacement of a Domain in the Rubella Virus P150 Replicase Protein by the Virus Capsid Protein

2009 ◽  
Vol 83 (8) ◽  
pp. 3549-3555 ◽  
Author(s):  
Wen-Pin Tzeng ◽  
Teryl K. Frey
Keyword(s):  
Rubella Virus ◽  
Rna Binding ◽  
Signal Sequence ◽  
Deletion Mutants ◽  
Replicase Gene ◽  
Wild Type ◽  
C Protein ◽  
Virus Capsid Protein ◽  
Functional Replacement ◽  
Arginine Rich Motif

ABSTRACT The rubella virus (RUBV) capsid (C) protein rescues mutants with a lethal deletion between two in-frame NotI sites in the P150 replicase gene, a deletion encompassing nucleotides 1685 to 2192 of the RUBV genome and amino acids (aa) 548 to 717 of P150 (which has a total length of 1,301 aa). The complete domain rescuable by the C protein was mapped to aa 497 to 803 of P150. Introduction of aa 1 to 277 of the C protein (lacking the C-terminal E2 signal sequence) between the NotI sites in the P150 gene in a replicon construct yielded a viable construct that synthesized viral RNA with wild-type kinetics, indicating that C and this region of P150 share a common function. Further genetic analysis revealed that an arginine-rich motif between aa 60 and 68 of the C protein was necessary for the rescue of ΔNotI deletion mutants and substituted for an arginine-rich motif between aa 731 and 735 of the P150 protein when the C protein was introduced into P150. Possible common functions shared by these arginine-rich motifs include RNA binding and interaction with cell proteins.

scholarly journals The fate of Hepatitis E virus capsid protein is regulated by an Arginine-Rich Motif

2021 ◽  
Author(s):  
Kévin Hervouet ◽  
Martin Ferrié ◽  
Maliki Ankavay ◽  
Claire Montpellier ◽  
Charline Camuzet ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Hepatitis E Virus ◽  
Nuclear Translocation ◽  
Hepatitis E ◽  
Particle Assembly ◽  
Humoral Immune ◽  
Antiviral Responses ◽  
Orf2 Protein ◽  
Molecular Determinants ◽  
Arginine Rich Motif

Producing multifunctional proteins is one of the major strategies developed by viruses to condense their genetic information. Here, we investigated the molecular determinants of the multifunctionality of hepatitis E virus (HEV) ORF2 capsid protein. We previously identified 3 isoforms of ORF2 which are partitioned in different subcellular compartments to perform distinct functions. Notably, the infectious ORF2 (ORF2i) protein is the structural component of the virion, whereas the genome-free secreted and glycosylated ORF2 proteins likely act as a humoral immune decoy. We identified a 5 amino acid Arginine-Rich Motif (ARM) located in the ORF2 N-terminal region as a central regulator of the subcellular localizations and functions of ORF2 isoforms. We showed that the ARM controls ORF2 nuclear translocation, promoting regulation of host antiviral responses. This motif also regulates the dual topology and functionality of ORF2 signal peptide, leading to the production of either cytosolic infectious ORF2i or reticular non-infectious glycosylated ORF2 forms. Furthermore, the ARM likely serves as a cleavage site of the glycosylated ORF2 protein. Finally, it promotes ORF2 membrane association that is likely essential for particle assembly. In conclusion, our observations highlight ORF2 ARM as a unique central regulator of ORF2 addressing that finely controls the HEV lifecycle.

scholarly journals A Conserved Arginine-Rich Motif within the Hypervariable N-Domain of Drosophila Centromeric Histone H3 (CenH3CID) Mediates BubR1 Recruitment

PLoS ONE ◽  
2010 ◽  
Vol 5 (10) ◽  
pp. e13747 ◽  
Author(s):  
Mònica Torras-Llort ◽  
Sònia Medina-Giró ◽  
Olga Moreno-Moreno ◽  
Fernando Azorín
Keyword(s):  
Histone H3 ◽  
Arginine Rich Motif
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