scholarly journals Energy-Independent Helicase Activity of a Viral Genome Packaging Motor

Biochemistry ◽  
2011 ◽  
Vol 51 (1) ◽  
pp. 391-400 ◽  
Author(s):  
Jenny R. Chang ◽  
Benjamin T. Andrews ◽  
Carlos E. Catalano
Keyword(s):  
Viral Genome ◽  
Helicase Activity ◽  
Genome Packaging

scholarly journals Energy Independent Helicase Activity of a Viral Genome Packaging Motor

2012 ◽  
Vol 102 (3) ◽  
pp. 642a
Author(s):  
Jenny R. Chang ◽  
Benjamin T. Andrews ◽  
Carlos E. Catalano
Keyword(s):  
Viral Genome ◽  
Helicase Activity ◽  
Genome Packaging

scholarly journals Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism

2017 ◽  
pp. gkw1354 ◽  
Author(s):  
Rui-Gang Xu ◽  
Huw T. Jenkins ◽  
Maria Chechik ◽  
Elena V. Blagova ◽  
Anna Lopatina ◽  
...  
Keyword(s):  
Viral Genome ◽  
Genome Packaging ◽  
Metal Catalysis ◽  
Catalysis Mechanism

Function of a viral genome packaging motor from bacteriophage T4 is insensitive to DNA sequence

2021 ◽  
Author(s):  
Douglas E. Smith ◽  
Youbin E. Mo ◽  
Nick Keller ◽  
Damian delToro ◽  
Neeti Ananthaswamy ◽  
...  
Keyword(s):  
Dna Sequence ◽  
Viral Genome ◽  
Bacteriophage T4 ◽  
Genome Packaging

scholarly journals Insights into Specific DNA Recognition during the Assembly of a Viral Genome Packaging Machine

2002 ◽  
Vol 9 (5) ◽  
pp. 981-991 ◽  
Author(s):  
Tonny de Beer ◽  
Jenny Fang ◽  
Marcos Ortega ◽  
Qin Yang ◽  
Levi Maes ◽  
...  
Keyword(s):  
Viral Genome ◽  
Dna Recognition ◽  
Genome Packaging ◽  
Packaging Machine

scholarly journals Intrinsically disordered region of influenza A NP regulates viral genome packaging via interactions with viral RNA and host PI(4,5)P 2

Virology ◽  
2016 ◽  
Vol 496 ◽  
pp. 116-126 ◽  
Author(s):  
Michinori Kakisaka ◽  
Kazunori Yamada ◽  
Akiko Yamaji-Hasegawa ◽  
Toshihide Kobayashi ◽  
Yoko Aida
Keyword(s):  
Viral Genome ◽  
Influenza A ◽  
Viral Rna ◽  
Genome Packaging ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Region

scholarly journals Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging

2016 ◽  
Vol 90 (9) ◽  
pp. 4593-4603 ◽  
Author(s):  
Tibor Füzik ◽  
Růžena Píchalová ◽  
Florian K. M. Schur ◽  
Karolína Strohalmová ◽  
Ivana Křížová ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Protein Interactions ◽  
Viral Genome ◽  
Virus Assembly ◽  
Protein Protein Interactions ◽  
Genome Packaging ◽  
Particle Assembly ◽  
Nuclear Trafficking ◽  
Virus Particles ◽  
Gag Polyprotein

ABSTRACTThe Gag polyprotein of retroviruses drives immature virus assembly by forming hexameric protein lattices. The assembly is primarily mediated by protein-protein interactions between capsid (CA) domains and by interactions between nucleocapsid (NC) domains and RNA. Specific interactions between NC and the viral RNA are required for genome packaging. Previously reported cryoelectron microscopy analysis of immature Mason-Pfizer monkey virus (M-PMV) particles suggested that a basic region (residues RKK) in CA may serve as an additional binding site for nucleic acids. Here, we have introduced mutations into the RKK region in both bacterial and proviral M-PMV vectors and have assessed their impact on M-PMV assembly, structure, RNA binding, budding/release, nuclear trafficking, and infectivity usingin vitroandin vivosystems. Our data indicate that the RKK region binds and structures nucleic acid that serves to promote virus particle assembly in the cytoplasm. Moreover, the RKK region appears to be important for recruitment of viral genomic RNA into Gag particles, and this function could be linked to changes in nuclear trafficking. Together these observations suggest that in M-PMV, direct interactions between CA and nucleic acid play important functions in the late stages of the viral life cycle.IMPORTANCEAssembly of retrovirus particles is driven by the Gag polyprotein, which can self-assemble to form virus particles and interact with RNA to recruit the viral genome into the particles. Generally, the capsid domains of Gag contribute to essential protein-protein interactions during assembly, while the nucleocapsid domain interacts with RNA. The interactions between the nucleocapsid domain and RNA are important both for identifying the genome and for self-assembly of Gag molecules. Here, we show that a region of basic residues in the capsid protein of the betaretrovirus Mason-Pfizer monkey virus (M-PMV) contributes to interaction of Gag with nucleic acid. This interaction appears to provide a critical scaffolding function that promotes assembly of virus particles in the cytoplasm. It is also crucial for packaging the viral genome and thus for infectivity. These data indicate that, surprisingly, interactions between the capsid domain and RNA play an important role in the assembly of M-PMV.

scholarly journals Function of a viral genome packaging motor from bacteriophage T4 is insensitive to DNA sequence

2020 ◽  
Vol 48 (20) ◽  
pp. 11602-11614
Author(s):  
Youbin Mo ◽  
Nicholas Keller ◽  
Damian delToro ◽  
Neeti Ananthaswamy ◽  
Stephen C Harvey ◽  
...  
Keyword(s):  
Dna Sequence ◽  
Motor Function ◽  
Optical Tweezers ◽  
Single Molecule ◽  
Dna Sequences ◽  
Viral Genome ◽  
Bacteriophage T4 ◽  
Repeated Measurements ◽  
Genome Packaging ◽  
Sequence Dependence

Abstract Many viruses employ ATP-powered motors during assembly to translocate DNA into procapsid shells. Previous reports raise the question if motor function is modulated by substrate DNA sequence: (i) the phage T4 motor exhibits large translocation rate fluctuations and pauses and slips; (ii) evidence suggests that the phage phi29 motor contacts DNA bases during translocation; and (iii) one theoretical model, the ‘B-A scrunchworm’, predicts that ‘A-philic’ sequences that transition more easily to A-form would alter motor function. Here, we use single-molecule optical tweezers measurements to compare translocation of phage, plasmid, and synthetic A-philic, GC rich sequences by the T4 motor. We observed no significant differences in motor velocities, even with A-philic sequences predicted to show higher translocation rate at high applied force. We also observed no significant changes in motor pausing and only modest changes in slipping. To more generally test for sequence dependence, we conducted correlation analyses across pairs of packaging events. No significant correlations in packaging rate, pausing or slipping versus sequence position were detected across repeated measurements with several different DNA sequences. These studies suggest that viral genome packaging is insensitive to DNA sequence and fluctuations in packaging motor velocity, pausing and slipping are primarily stochastic temporal events.

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