Subcellular localization of the 28 kDa protein of the triple-gene-block of bamboo mosaic potexvirus.

Chang, Ban‐Yang; Lin, Na-Sheng; Liou, Dann-Ying; Chen, Jia-Perng; Liou, Gunn‐Guang; Hsu, Yau‐Heiu

doi:10.1099/0022-1317-78-5-1175

Cited by 46 publications

(36 citation statements)

References 24 publications

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“…Specifically, the BNYVV (15) and PCV (16) TGB1 proteins localize to plasmodesmata, while the BSMV TGB1 foci are often present as paired foci that appear to traverse the walls of adjacent cells. This localization pattern contrasts with that of the smaller TGB1 proteins of the potexviruses Bamboo mosaic virus (8), Foxtail mosaic virus (50), and PVX (10) that do not In each experiment, 100 BY-2 protoplasts were observed at 23 to 26 h posttransfection. The results shown are the mean and the standard deviations of three separate experiments and are shown for sites of subcellular localization.…”

Section: Vol 75 2001mentioning

confidence: 78%

Interactions of the TGB1 Protein during Cell-to-Cell Movement of Barley Stripe Mosaic Virus

Lawrence

Jackson

2001

J Virol

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). We have now extended these analyses by engineering a fusion of GFP to TGB1 to examine the expression and interactions of this protein during infection. BSMV derivatives containing the TGB1 fusion were able to move from cell to cell and establish local lesions in Chenopodium amaranticolor and systemic infections of Nicotiana benthamiana and barley. In these hosts, the GFP-TGB1 fusion protein exhibited a temporal pattern of expression along the advancing edge of the infection front. Microscopic examination of the subcellular localization of the GFP-TGB1 protein indicated an association with the endoplasmic reticulum and with plasmodesmata. The subcellular localization of the TGB1 protein was altered in infections in which sitespecific mutations were introduced into the six conserved regions of the helicase domain and in mutants unable to express the TGB2 and/or TGB3 proteins. These results are compatible with a model suggesting that movement requires associations of the TGB1 protein with cytoplasmic membranes that are facilitated by the TGB2 and TGB3 proteins.

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Section: Vol 75 2001mentioning

confidence: 78%

Interactions of the TGB1 Protein during Cell-to-Cell Movement of Barley Stripe Mosaic Virus

Lawrence

Jackson

2001

J Virol

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“…(B) Western blot analysis of TGBp1. Total proteins were extracted from the BaMV-infected protoplasts at 2 days p.i., separated by 12 % SDS-PAGE, blotted onto a PVDF membrane and probed with polyclonal antiserum against TGBp1 (Chang et al, 1997). The numbers shown in the left margin indicate the apparent M r in kDa.…”

Section: Discussionmentioning

confidence: 99%

“…The numbers shown in the left margin indicate the apparent M r in kDa. Lane 1, TGBp1 of BaMV purified from an E. coli overexpression system (Chang et al, 1997); lanes 2-7, as in (A).…”

Section: Discussionmentioning

confidence: 99%

“…Methods for total protein extraction and Western blot analysis were as previously reported (Lin et al, 1996;Chang et al, 1997) except that an ECL detection system was adopted (Amersham).…”

Section: Methodsmentioning

confidence: 99%

“…Although BaMV TGBp1 belongs to the RNA helicase superfamily I (Kadare & Haenni, 1997;Morozov et al, 1999;Liou et al, 2000), Arg-16 and Arg-21, which are located outside the seven conserved motifs of the superfamily I RNA helicase, are also critical for the NTPase activity of TGBp1 (Liou et al, 2000). TGBp1s of potexviruses are in fact mainly associated with cytoplasmic inclusions in infected tissues (Chang et al, 1997;Davies et al, 1993;Rouleau et al, 1994). The TGBp1 obtained from the cytoplasmic inclusions also possesses NTP-binding and NTPase activities but lacks the RNA-binding activity (Liou et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

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Arg-16 and Arg-21 in the N-terminal region of the triple-gene-block protein 1 of Bamboo mosaic virus are essential for virus movement

Lin

Chang

Liao

et al. 2004

Journal of General Virology

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The protein encoded by the first gene of the triple gene block (TGBp1) of potexviruses is required for movement of the viruses. It has been reported that single ArgRAla substitutions at position 11, 16 or 21 of TGBp1 of Bamboo mosaic virus (BaMV) eliminate its RNA-binding activity, while substitutions at position 16 or 21 only affect its NTPase activity (Liou et al., Virology 277, 336-344, 2000). However, it remains unclear whether these ArgRAla substitutions also affect the movement of BaMV in plants. To address this question, six mutants of BaMV, each containing either a single-or a double-alanine substitution at Arg-11, Arg-16 and Arg-21 of TGBp1, were constructed and used to infect Chenopodium quinoa and Nicotiana benthamiana. We found that all of the BaMV mutants were able to replicate in protoplasts of N. benthamiana. However, only the mutant with an Arg-11RAla substitution in TGBp1 remained capable of movement from cell to cell in plants. Mutants with Arg-16, Arg-21 or both Arg-16 and Arg-21 of TGBp1 replaced with alanine were defective in virus movement. This defect was suppressed when a wild-type TGBp1 allele was co-introduced into the cells using a novel satellite replicon. The ability to trans-complement the movement defect by the wild-type TGBp1 strongly suggests that the ArgRAla substitution at position 16 or 21 of TGBp1, which diminishes the RNA-binding and NTPase activities of TGBp1, also eliminates the capability of BaMV to move from cell to cell in host plants.

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The First Triple Gene Block Protein of Peanut Clump Virus Localizes to the Plasmodesmata during Virus Infection

et al. 1999

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The subcellular localization of the first triple gene block protein (TGBp1) of peanut clump pecluvirus (PCV) was studied by subcellular fractionation and immunogold cytochemistry using TGBp1-specific antibodies raised against a fusion protein expressed in and purified from bacteria. In the inoculated and apical leaves of virus-infected Nicotiana benthamiana, TGBp1 localized to the cell wall and P30 fractions. Electron microscopy of immunogold-decorated ultrathin sections of the infected leaf tissue revealed TGBp1-specific labeling of the plasmodesmata joining mesophyll cells. In longitudinal sections of the plasmodesmata, the TGBp1-specific labeling was most commonly associated with the plasmodesmal collar region. In transgenic N. benthamiana, which constitutively expressed TGBp1, no TGBp1-specific immunogold labeling of plasmodesmata was observed, but plasmodesmata were gold decorated when the transgenic plants were infected with a TGBp1-defective PCV mutant, indicating that factors induced by the virus infection target and/or anchor the transgene TGBp1 to the plasmodesmata.

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Subcellular localization of the 28 kDa protein of the triple-gene-block of bamboo mosaic potexvirus.

Cited by 46 publications

References 24 publications

Interactions of the TGB1 Protein during Cell-to-Cell Movement of Barley Stripe Mosaic Virus

Interactions of the TGB1 Protein during Cell-to-Cell Movement of Barley Stripe Mosaic Virus

Arg-16 and Arg-21 in the N-terminal region of the triple-gene-block protein 1 of Bamboo mosaic virus are essential for virus movement

The First Triple Gene Block Protein of Peanut Clump Virus Localizes to the Plasmodesmata during Virus Infection

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