Interaction of the host protein NbDnaJ with Potato virus X minus-strand stem-loop 1 RNA and capsid protein affects viral replication and movement

Cho, Sang-Yun; Cho, Won Kyong; Sohn, Seong-Han; Kim, Kook‐Hyung

doi:10.1016/j.bbrc.2011.11.137

Cited by 29 publications

(15 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Spots 1, 17 and 34 were identified as dnaJ-like protein, heat shock protein HSP26 and zinc finger (C3HC4-type RING finger) protein–like, respectively. These proteins are linked to stress response in plants and play important roles in various physiological processes (Cho et al 2012 ; Yuan et al 2013 ). It has been reported that some HSPs are involved in wheat resistance reaction against F. graminearum attack (Wang et al 2005 ; Schweiger et al 2013 ), and Lund et al ( 2001 ) reported the first instance where a plant sHSP has been shown to be phosphorylated in vivo.…”

Section: Resultsmentioning

confidence: 99%

Identification of putative phosphoproteins in wheat spikes induced by Fusarium graminearum

Ding

Yang²,

Yang

et al. 2015

Planta

View full text Add to dashboard Cite

Main conclusionPhosphorylation and dephosphorylation events were initiated in wheat scab resistance. The putative FHB-responsive phosphoproteins are mainly involved in three functional groups and contain at least one tyrosine, serine, or threonine phosphorylation site.Fusarium head blight (FHB), caused by Fusarium graminearum, is a severe disease in wheat. Protein phosphorylation plays an important role in plant–pathogen interactions, however, a global analysis of protein phosphorylation in response to FHB infection remains to be explored. To study the effect of FHB on the phosphorylation state of wheat proteins, proteins extracted from spikes of a resistant wheat cultivar after 6 h of inoculation with F. graminearum or sterile H2O were separated by two-dimensional gel electrophoresis, and then the immunodetection of putative phosphoproteins was conducted by Western blotting using specific anti-phosphotyrosine antibody, anti-phosphothreonine antibody and anti-phosphoserine antibody. A total of 35 phosphorylated signals was detected and protein identities of 28 spots were determined. Functional categorization showed that the putative FHB-responsive phosphoproteins were mainly involved in defense/stress response, signal transduction, and metabolism. The phosphorylation status of proteins associated with signaling pathways mediated by salicylic acid, calcium ions, small GTPase, as well as with detoxification, reactive oxygen species scavenging, antimicrobial compound synthesis, and cell wall fortification was regulated in wheat spikes in response to F. graminearum infection. The present study reveals dynamics of wheat phosphoproteome in response to F. graminearum infection and suggests an important role of protein Ser/Thr/Tyr phosphorylation in fundamental mechanisms of wheat scab resistance.Electronic supplementary materialThe online version of this article (doi:10.1007/s00425-015-2441-y) contains supplementary material, which is available to authorized users.

show abstract

Section: Resultsmentioning

confidence: 99%

Identification of putative phosphoproteins in wheat spikes induced by Fusarium graminearum

Ding

Yang²,

Yang

et al. 2015

Planta

View full text Add to dashboard Cite

show abstract

“…As indicated by deletion assay, the C-terminal region of NbDnaJ is essential for the interaction with PVX CP (Cho et al, 2012c). According to the latter study, when NbDnaJ is overexpressed in transient assay, PVX movement is suppressed.…”

Section: Host Cellular Factors Interacting With Viral Rna Elements Inmentioning

confidence: 99%

Understanding the intracellular trafficking and intercellular transport of potexviruses in their host plants

2014

Self Cite

View full text Add to dashboard Cite

The movement of potexviruses through the cytoplasm to plasmodesmata (PD) and through PD to adjacent cells depends on the viral and host cellular proteins. Potexviruses encode three movement proteins [referred to as the triple gene block (TGB1–3)]. TGB1 protein moves cell-to-cell through PD and requires TGB2 and TGB3, which are endoplasmic reticulum (ER)-located proteins. TGB3 protein directs the movement of the ER-derived vesicles induced by TGB2 protein from the perinuclear ER to the cortical ER. TGB2 protein physically interacts with TGB3 protein in a membrane-associated form and also interacts with either coat protein (CP) or TGB1 protein at the ER network. Recent studies indicate that potexvirus movement involves the interaction between TGB proteins and CP with host proteins including membrane rafts. A group of host cellular membrane raft proteins, remorins, can serve as a counteracting membrane platform for viral ribonucleoprotein (RNP) docking and can thereby inhibit viral movement. The CP, which is a component of the RNP movement complex, is also critical for viral cell-to-cell movement through the PD. Interactions between TGB1 protein and/or the CP subunit with the 5′-terminus of genomic RNA [viral RNA (vRNA)] form RNP movement complexes and direct the movement of vRNAs through the PD. Recent studies show that tobacco proteins such as NbMPB2C or NbDnaJ-like proteins interact with the stem-loop 1 RNA located at the 5′-terminus of Potato virus X vRNA and regulate intracellular as well as intercellular movement. Although several host proteins that interact with vRNAs or viral proteins and that are crucial for vRNA transport have been screened and characterized, additional host proteins and details of viral movement remain to be characterized. In this review, we describe recent progress in understanding potexvirus movement within and between cells and how such movement is affected by interactions between vRNA/proteins and host proteins.

show abstract

“…NbDnaJ protein was shown by an electro-mobility shift assay to interact specifically with the minus-strand SL1 in vitro . NbDnaJ also interacts with PVX CP in planta , and negatively affects the systemic movement of the virus (Cho et al, 2012c). NbMPB2Cb, another SL1-interacting protein, interacts with PVX CP, TGBp1, and TGBp2 in planta , and negatively regulates the systemic movement of PVX (Cho et al, 2012a).…”

Section: Host Rbps Involved In the Intercellular Movement Of Vrnasmentioning

confidence: 99%

Host and viral RNA-binding proteins involved in membrane targeting, replication and intercellular movement of plant RNA virus genomes

2014

View full text Add to dashboard Cite

Many plant viruses have positive-strand RNA [(+)RNA] as their genome. Therefore, it is not surprising that RNA-binding proteins (RBPs) play important roles during (+)RNA virus infection in host plants. Increasing evidence demonstrates that viral and host RBPs play critical roles in multiple steps of the viral life cycle, including translation and replication of viral genomic RNAs, and their intra- and intercellular movement. Although studies focusing on the RNA-binding activities of viral and host proteins, and their associations with membrane targeting, and intercellular movement of viral genomes have been limited to a few viruses, these studies have provided important insights into the molecular mechanisms underlying the replication and movement of viral genomic RNAs. In this review, we briefly overview the currently defined roles of viral and host RBPs whose RNA-binding activity have been confirmed experimentally in association with their membrane targeting, and intercellular movement of plant RNA virus genomes.

show abstract

Interaction of the host protein NbDnaJ with Potato virus X minus-strand stem-loop 1 RNA and capsid protein affects viral replication and movement

Cited by 29 publications

References 29 publications

Identification of putative phosphoproteins in wheat spikes induced by Fusarium graminearum

Identification of putative phosphoproteins in wheat spikes induced by Fusarium graminearum

Understanding the intracellular trafficking and intercellular transport of potexviruses in their host plants

Host and viral RNA-binding proteins involved in membrane targeting, replication and intercellular movement of plant RNA virus genomes

Contact Info

Product

Resources

About