Chloroplast phosphoglycerate kinase, a gluconeogenetic enzyme, is required for efficient accumulation of Bamboo mosaic virus

Abstract

The tertiary structure in the 3′-untranslated region (3′-UTR) of Bamboo mosaic virus (BaMV) RNA is known to be involved in minus-strand RNA synthesis. Proteins found in the RNA-dependent RNA polymerase (RdRp) fraction of BaMV-infected leaves interact with the radio labeled 3′-UTR probe in electrophoretic mobility shift assays (EMSA). Results derived from the ultraviolet (UV) cross-linking competition assays suggested that two cellular factors, p43 and p51, interact specifically with the 3′-UTR of BaMV RNA. p43 and p51 associate with the poly(A) tail and the pseudoknot of the BaMV 3′-UTR, respectively. p51-containing extracts specifically down-regulated minus-strand RNA synthesis when added to in vitro RdRp assays. LC/MS/MS sequencing indicates that p43 is a chloroplast phosphoglycerate kinase (PGK). When the chloroplast PKG levels were knocked down in plants, using virus-induced gene silencing system, the accumulation level of BaMV coat protein was also reduced.

Influence of Host Chloroplast Proteins on Tobacco mosaic virus Accumulation and Intercellular Movement

“…In addition, modifying levels of particular host chloroplast proteins alters the accumulation of some viruses. The chloroplast protein, phosphoglycerate kinase, is required for the accumulation of Bamboo mosaic virus, a virus related to PVX (Lin et al, 2007). Also, chloroplast proteins are implicated in defending against infections.…”

A Violaxanthin Deepoxidase Interacts with a Viral Suppressor of RNA Silencing to Inhibit Virus Amplification

“…kinase gene (cPGK) or mislocalization of cPGK protein reduced the potexvirus Bamboo mosaic virus accumulation (Lin et al, 2007;Cheng et al, 2013). NRIP1 is responsible for pathogen recognition through its ability to interact with both the plant N immune receptor and the 50-kD helicase (p50) domain of Tobacco mosaic virus (TMV), and silencing of NRIP1 facilitated TMV infection (Caplan et al, 2008).…”

Suppression of Bamboo Mosaic Virus Accumulation by a Putative Methyltransferase in Nicotiana benthamiana

“…Also, proper targeting of PNbMTS1 may be relevant to its viral suppression function. The chloroplast membrane has been suggested to be the site for BaMV replication based on the finding that the chloroplast phosphoglycerate kinase can assist viral replication (26). However, direct evidence for this is still lacking.…”

“…These factors are diverse, and many of them are involved in the metabolism of proteins, nucleic acids, and lipids. With respect to BaMV, binding of the chloroplast phosphoglycerate kinase to the 3Ј untranslated region was found to be required for efficient accumulation of BaMV coat protein in Nicotiana benthamiana (26).…”