The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase

J. F. Murphy; R. E. Rhoads; A. G. Hunt; J. G. Shaw

doi:10.1016/0042-6822(90)90405-G

The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase

J. F. Murphy, R. E. Rhoads, A. G. Hunt, J. G. Shaw

Research output: Contribution to journal › Article › peer-review

118 Scopus citations

Abstract

Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamide gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.

Original language	English
Pages (from-to)	285-288
Number of pages	4
Journal	Virology
Volume	178
Issue number	1
DOIs	https://doi.org/10.1016/0042-6822(90)90405-G
State	Published - Sep 1990

Bibliographical note

Funding Information:
We thank Wrlliam G. Dougherty for providing polyclonal and monoclonal antisera to the 49.kDa proternase and Thomas P. Pirone for provrding antrserum to TEV. This work was supported by Grant 4E021 from the Unrversrty of Kentucky Tobacco and Health Research Institute and Grant 85.CRCR-1-1536 from the U.S. Department of Agriculture Competitive Grants Program.

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

ASJC Scopus subject areas

Virology

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10.1016/0042-6822(90)90405-G

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title = "The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase",

abstract = "Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamide gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.",

author = "Murphy, {J. F.} and Rhoads, {R. E.} and Hunt, {A. G.} and Shaw, {J. G.}",

note = "Funding Information: We thank Wrlliam G. Dougherty for providing polyclonal and monoclonal antisera to the 49.kDa proternase and Thomas P. Pirone for provrding antrserum to TEV. This work was supported by Grant 4E021 from the Unrversrty of Kentucky Tobacco and Health Research Institute and Grant 85.CRCR-1-1536 from the U.S. Department of Agriculture Competitive Grants Program. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1990",

month = sep,

doi = "10.1016/0042-6822(90)90405-G",

language = "English",

volume = "178",

pages = "285--288",

number = "1",

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T1 - The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase

AU - Murphy, J. F.

AU - Rhoads, R. E.

AU - Hunt, A. G.

AU - Shaw, J. G.

N1 - Funding Information: We thank Wrlliam G. Dougherty for providing polyclonal and monoclonal antisera to the 49.kDa proternase and Thomas P. Pirone for provrding antrserum to TEV. This work was supported by Grant 4E021 from the Unrversrty of Kentucky Tobacco and Health Research Institute and Grant 85.CRCR-1-1536 from the U.S. Department of Agriculture Competitive Grants Program. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1990/9

Y1 - 1990/9

N2 - Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamide gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.

AB - Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamide gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.

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The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase

Abstract

Bibliographical note

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