The TMV movement protein: Role of the C-terminal 73 amino acids in subcellular localization and function

Anne Berna*, Ron Gafny, Shmuel Wolf, William J. Lucas, Curtis A. Holt, Roger N. Beachy

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

The role of the C-terminal one-third of the tobacco mosaic virus (TMV) 30-kDa movement protein (MP) on its subcellular localization and on virus spread was investigated. We have constructed eight cDNAs encoding MPs with variable size deletions from the C-terminal end. Expression of the truncated proteins was verified in recombinant yeast using an antiserum directed to a synthetic peptide corresponding to 21 amino acids near the N-terminal end of the MP. In transgenic tobacco plants, MP from which more than 55 amino acids were deleted no longer accumulated in the cell wall fraction of a cellular extract, where the complete MP accumulates. Dye diffusion studies showed that both unmodified and modified MPs that accumulate in the cell wall fraction are able to alter plasmodesmatal size exclusion limits. Biological function of the modified MPs was tested in the transgenic plants with the TMV thermosensitive mutant Lsl and a TMV genomic RNA transcript lacking a functional MP. There was a correlation between the cell wall localization of the modified MPs and its ability to potentiate virus spread. The results presented here demonstrate the dispensability of the C-terminal 55 amino acids of the MP in its subcellular localization in tobacco plants and its role in virus movement. Moreover, our results show that a stretch of 19 amino acids (195 to 213) is essential for localization of the MP to the cell wall fraction of plant cells.

Original languageAmerican English
Pages (from-to)682-689
Number of pages8
JournalVirology
Volume182
Issue number2
DOIs
StatePublished - Jun 1991
Externally publishedYes

Bibliographical note

Funding Information:
We thank C. Smith and K. Kafka, Monsanto Company (St. Louis, MO), for preparing oligopeptide and oligonucleotides; Dr. T. Vernet, (Toronto, Canada), for the yeast shuttle vector; Dr. M. R. Chevallier, IBMP (Strasbourg, France), for yeast strains; Dr. T. Godefroy-Col- burn, IBMP (Strasbourg, France), for stimulating discussions; and Dr. F. Bernier, Universite Lava1 (QuBbec, Canada), for critical reading of the manuscript. This research was supported by NSF grants to R.N.B. (DMB 8717012) and W.J.L. (DMB 8703624). A.B. was the recipient of an EMBO long-term Fellowship and R.G. was supported by a BARD Fellowship.

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