AI Article Synopsis

  • Mung bean yellow mosaic India virus (MYMIV) has a bipartite genome consisting of two components of single-stranded, circular DNA crucial for its replication process.
  • The study focused on the role of the host protein, Replication Protein A (RPA), specifically the RPA32 kDa subunit, which was found to interact with the viral replication protein (MYMIV-Rep) and influence its activity.
  • Evidence suggests that RPA32 enhances certain functions of MYMIV-Rep while modulating others, ultimately contributing to efficient viral DNA replication in a plant-based system.

Article Abstract

Mung bean yellow mosaic India virus (MYMIV) is a member of genus begomoviridae and its genome comprises of bipartite (two components, namely DNA-A and DNA-B), single-stranded, circular DNA of about 2.7 kb. During rolling circle replication (RCR) of the DNA, the stability of the genome and maintenance of the stem-loop structure of the replication origin is crucial. Hence the role of host single-stranded DNA-binding protein, Replication protein A (RPA), in the RCR of MYMIV was examined. Two RPA subunits, namely the RPA70 kDa and RPA32 kDa, were isolated from pea and their roles were validated in a yeast system in which MYMIV DNA replication has been modelled. Here, we present evidences that only the RPA32 kDa subunit directly interacted with the carboxy terminus of MYMIV-Rep both in vitro as well as in yeast two-hybrid system. RPA32 modulated the functions of Rep by enhancing its ATPase and down regulating its nicking and closing activities. The possible role of these modulations in the context of viral DNA replication has been discussed. Finally, we showed the positive involvement of RPA32 in transient replication of the plasmid DNA bearing MYMIV replication origin using an in planta based assay.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807949PMC
http://dx.doi.org/10.1093/nar/gkl1088DOI Listing

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