Novel interactions of cardamom mosaic virus VPg with cardamom histones H3 and H4
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Novel interactions of cardamom mosaic virus VPg with cardamom histones H3 and H4 Sankara Naynar Palani1 · Ramamoorthy Sankaranarayanan1 · Jebasingh Tennyson1 Received: 9 December 2019 / Accepted: 29 August 2020 © King Abdulaziz City for Science and Technology 2020
Abstract The host genome targeting potyviral proteins is sparsely reported. Viral genome-linked protein (VPg) is a multifaceted protein known for its interactions with a suite of host proteins, guides essential viral life cycle processes such as genome replication, translation, genome packing, and antiviral defence. Besides, VPg also plays a crucial role in assisting the transport of nuclear inclusion a protease (NIa protease) into the host nucleus. Apart from that, the role of VPg in the nucleus of the cognate host is not clear. Although NIa protease has been reported for DNase activity, the molecular mechanisms underlying host genome accessibility are not yet understood completely. Here, we employed yeast two hybrid assays to test the cardamom histones H3 and H4 interaction with the VPg and NIa protease of macluravirus cardamom mosaic virus (CdMV). Although CdMV NIa protease has the putative histone-binding ER motif of MYST histone acetyltransferase, it did not interact with host histones H3 and H4. Surprisingly, CdMV VPg displayed strong interaction with histone proteins H3 and H4. Leucine prototrophy and β-galactosidase assays were performed which validated VPg interaction with histones. To the best of our knowledge, this study is the first report for the multipartnered potyvirid protein VPg interaction with host histones H3 and H4. Keywords VPg · NIa protease · Cardamom mosaic virus · ER motif · Histones
Introduction Cardamom mosaic virus (CdMV), a species of Macluravirus genus, belongs to the family Potyviridae (Jacob and Usha 2001). Macluraviruses codes for a long polyprotein which is majorly cleaved by nuclear inclusion a protease (NIa protease) (Palani et al. 2018). So far, a plethora of molecular studies has reported the protease activity of NIa protease (Garcia et al. 1992; Dougherty and Semler 1993, Joseph and Savithri 2000; Ray and Hema 2016). However, its role in the host nucleus is still unexplored. The DNase activity of Pepper vein banding virus (PVBV) NIa protease has been believed to degrade the host genome to suppress the host defence (Anindya and Savithri 2004; Revers and Garcia 2015). Since the eukaryotic genome is packed as nucleosomes, the action of NIa protease may commence with chromatin remodelling. Interestingly, sequence comparison * Jebasingh Tennyson [email protected] 1
Department of Plant Sciences, School of Biological Sciences, Madurai Kamaraj University, Madurai, Tamil Nadu 625021, India
showed that essential amino acids of histone-binding ER (Esa1-Rpd3) motif of MYST family are found in CdMV and a few other macluravirus NIa proteases (Fig. 1a). MYST family of histone acetyltransferases (HAT) preferably binds to histones of H3 and H4 (Adachi et al. 2002). The role of this putative ER motif in CdM
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