Coat protein of cauliflower mosaic virus binds to ssDNA

Thompson, Sunnie R.; Melcher, Ulrich

doi:10.1099/0022-1317-74-6-1141

Cited by 6 publications

(1 citation statement)

References 34 publications

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“…Several reports have described the interaction between CaMV CP and nucleic acids (7,9,15,24,48) but none have described the specific interaction between CP and RNA that is . FIG.…”

Section: Discussionmentioning

confidence: 99%

Interaction of the Cauliflower Mosaic Virus Coat Protein with the Pregenomic RNA Leader

Guerra‐Peraza

Tapia

Höhn

et al. 2000

J Virol

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Using the yeast three-hybrid system, the interaction of the Cauliflower mosaic virus (CaMV) pregenomic 35S RNA (pgRNA) leader with the viral coat protein, its precursor, and a series of derivatives was studied. The purine-rich domain in the center of the pgRNA leader was found to specifically interact with the coat protein.The zinc finger motif of the coat protein and the preceding basic domain were essential for this interaction. Removal of the N-terminal portion of the basic domain led to loss of specificity but did not affect the strength of the interaction. Mutations of the zinc finger motif abolished not only the interaction with the RNA but also viral infectivity. In the presence of the very acidic C-terminal domain, which is part of the preprotein but is not present in the mature CP, the interaction with the RNA was undetectable.

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“…Several reports have described the interaction between CaMV CP and nucleic acids (7,9,15,24,48) but none have described the specific interaction between CP and RNA that is . FIG.…”

Section: Discussionmentioning

confidence: 99%

Interaction of the Cauliflower Mosaic Virus Coat Protein with the Pregenomic RNA Leader

Guerra‐Peraza

Tapia

Höhn

et al. 2000

J Virol

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Viral Protein–Nucleic Acid Interaction: South (North)-Western Blot

Liu

2008

Plant Virology Protocols

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Maize streak virus (MSV) genome has four open reading frames. C1 and C2 encoded by the complementary sense are required for virus replication, while V1 and V2 encoded by virion sense are required for infectivity. V1 encodes movement protein (MP), while V2 encodes coat protein (CP). Deletion or mutation of MSV CP does not prevent virus replication in single cells or protoplasts but leads to a loss of infectivity in the inoculated plant suggesting that MSV CP is required for virus movement. Towards understanding the role of MSV CP and MP in virus movement, the interaction of MSV CP and MP with viral DNA was investigated using the South-western assay. Wild type and truncated MSV CPs and MP were expressed in E. coli and the expressed CPs and MP were used to investigate interaction with single-stranded (ss) and double-stranded (ds) DNA. The results showed MSV MP does not bind DNA in the assay while MSV CP bound ss and ds viral and uidA DNA in a sequence non-specific manner.

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