scholarly journals Retroviral RNA Dimerization: From Structure to Functions

2018 ◽  
Vol 9 ◽  
Author(s):  
Noé Dubois ◽  
Roland Marquet ◽  
Jean-Christophe Paillart ◽  
Serena Bernacchi
Keyword(s):  
Rna Dimerization

Binding of Aminoglycoside Antibiotics to the Duplex Form of the HIV-1 Genomic RNA Dimerization Initiation Site

2008 ◽  
Vol 47 (22) ◽  
pp. 4110-4113 ◽  
Author(s):  
Séverine Freisz ◽  
Kathrin Lang ◽  
Ronald Micura ◽  
Philippe Dumas ◽  
Eric Ennifar
Keyword(s):  
Initiation Site ◽  
Aminoglycoside Antibiotics ◽  
Genomic Rna ◽  
Rna Dimerization ◽  
Hiv 1 ◽  
Dimerization Initiation Site

scholarly journals Structure of the 30 kDa HIV-1 RNA Dimerization Signal by a Hybrid Cryo-EM, NMR, and Molecular Dynamics Approach

Structure ◽  
2018 ◽  
Vol 26 (3) ◽  
pp. 490-498.e3 ◽  
Author(s):  
Kaiming Zhang ◽  
Sarah C. Keane ◽  
Zhaoming Su ◽  
Rossitza N. Irobalieva ◽  
Muyuan Chen ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Rna Dimerization ◽  
Hiv 1

scholarly journals Opening of the TAR hairpin in the HIV-1 genome causes aberrant RNA dimerization and packaging

Retrovirology ◽  
2012 ◽  
Vol 9 (1) ◽  
Author(s):  
Atze T Das ◽  
Martine M Vrolijk ◽  
Alex Harwig ◽  
Ben Berkhout
Keyword(s):  
Rna Dimerization ◽  
Aberrant Rna ◽  
Hiv 1

scholarly journals Functional Characterization of Yeast Telomerase RNA Dimerization

2007 ◽  
Vol 282 (26) ◽  
pp. 18857-18863 ◽  
Author(s):  
Clay L. Gipson ◽  
Zhong-Tao Xin ◽  
Shamika C. Danzy ◽  
Tristram G. Parslow ◽  
Hinh Ly
Keyword(s):  
Functional Characterization ◽  
Telomerase Rna ◽  
Rna Dimerization ◽  
Yeast Telomerase

scholarly journals trans-Acting Inhibition of Genomic RNA Dimerization by Rous Sarcoma Virus Matrix Mutants

2001 ◽  
Vol 75 (1) ◽  
pp. 260-268 ◽  
Author(s):  
Rachel A. Garbitt ◽  
Jessica A. Albert ◽  
Michelle D. Kessler ◽  
Leslie J. Parent
Keyword(s):  
Rous Sarcoma Virus ◽  
Single Amino Acid ◽  
Genomic Rna ◽  
Wild Type ◽  
Protein Fusion ◽  
Dimer Formation ◽  
Rna Sequence ◽  
Rna Dimerization ◽  
Rous Sarcoma ◽  
Sarcoma Virus

ABSTRACT The genomic RNA of retroviruses exists within the virion as a noncovalently linked dimer. Previously, we identified a mutant of the viral matrix (MA) protein of Rous sarcoma virus that disrupts viral RNA dimerization. This mutant, Myr1E, is modified at the N terminus of MA by the addition of 10 amino acids from the Src protein, resulting in the production of particles containing monomeric RNA. Dimerization is reestablished by a single amino acid substitution that abolishes myristylation (Myr1E−). To distinguish between cis andtrans effects involving Myr1E, additional mutations were generated. In Myr1E.cc and Myr1E−.cc, different nucleotides were utilized to encode the same protein as Myr1E and Myr1E−, respectively. The alterations in RNA sequence did not change the properties of the viral mutants. Myr1E.ATG− was constructed so that translation began at the gag AUG, resulting in synthesis of the wild-type Gag protein but maintenance of the src RNA sequence. This mutant had normal infectivity and dimeric RNA, indicating that thesrc sequence did not prevent dimer formation. All of the src-containing RNA sequences formed dimers in vitro. Examination of MA-green fluorescent protein fusion proteins revealed that the wild-type and mutant MA proteins Myr1E.ATG−, Myr1E−, and Myr1E−.cc had distinctly different patterns of subcellular localization compared with Myr1E and Myr1E.cc MA proteins. This finding suggests that proper localization of the MA protein may be required for RNA dimer formation and infectivity. Taken together, these results provide compelling evidence that the genomic RNA dimerization defect is due to a trans-acting effect of the mutant MA proteins.

scholarly journals Duplication of the Primary Encapsidation and Dimer Linkage Region of Human Immunodeficiency Virus Type 1 RNA Results in the Appearance of Monomeric RNA in Virions

2001 ◽  
Vol 75 (6) ◽  
pp. 2557-2565 ◽  
Author(s):  
Jun-ichi Sakuragi ◽  
Tatsuo Shioda ◽  
Antonito T. Panganiban
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Intramolecular Interaction ◽  
Genomic Rna ◽  
Virion Assembly ◽  
Virus Particles ◽  
Rna Dimerization ◽  
Immunodeficiency Virus ◽  
Dimer Linkage

ABSTRACT The dimerization initiation site (DIS) and the dimer linkage sequences (DLS) of human immunodeficiency virus type 1 have been shown to mediate in vitro dimerization of genomic RNA. However, the precise role of the DIS-DLS region in virion assembly and RNA dimerization in virus particles has not been fully elucidated, since deletion or mutation of the DIS-DLS region also abolishes the packaging ability of genomic RNA. To characterize the DIS-DLS region without altering packaging ability, we generated mutant constructs carrying a duplication of approximately 1,000 bases including the encapsidation signal and DIS-DLS (E/DLS) region. We found that duplication of the E/DLS region resulted in the appearance of monomeric RNA in virus particles. No monomers were observed in virions of mutants carrying the E/DLS region only at ectopic positions. Monomers were not observed whenpol or env regions were duplicated, indicating an absolute need for two intact E/DLS regions on the same RNA for generating particles with monomeric RNA. These monomeric RNAs were most likely generated by intramolecular interaction between two E/DLS regions on one genome. Moreover, incomplete genome dimerization did not affect RNA packaging and virion formation. Examination of intramolecular interaction between E/DLS regions could be a convenient tool for characterizing the E/DLS region in virion assembly and RNA dimerization within virus particles.

Oligonucleotide-Mediated Inhibition of Genomic RNA Dimerization of HIV-1 Strains MAL and LAI: A Comparative Analysis

1998 ◽  
Vol 8 (6) ◽  
pp. 517-529 ◽  
Author(s):  
J. STEPHEN LODMELL ◽  
JEAN-CHRISTOPHE PAILLART ◽  
DELPHINE MIGNOT ◽  
BERNARD EHRESMANN ◽  
CHANTAL EHRESMANN ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Genomic Rna ◽  
Rna Dimerization ◽  
Hiv 1
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