HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

Alexander V. Karasev; Anna S. Kashina; Vladimir I. Gelfand; Valerian V. Dolja

doi:10.1016/0014-5793(92)80578-5

HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

Alexander V. Karasev, Anna S. Kashina, Vladimir I. Gelfand, Valerian V. Dolja^*

^*Corresponding author for this work

Cell & Developmental Biology

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

54 Scopus citations

Abstract

Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603-610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 × 10^-7 M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of α- and β-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.

Original language	English (US)
Pages (from-to)	12-14
Number of pages	3
Journal	FEBS Letters
Volume	304
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(92)80578-5
State	Published - Jun 8 1992

Keywords

Cell-to-cell movement
Microtubule-associated protein
Plant virus

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(92)80578-5

Cite this

@article{f20741b4efcd4d97a8ea308c444470ce,

title = "HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein",

abstract = "Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603-610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 × 10-7 M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of α- and β-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.",

keywords = "Cell-to-cell movement, Microtubule-associated protein, Plant virus",

author = "Karasev, {Alexander V.} and Kashina, {Anna S.} and Gelfand, {Vladimir I.} and Dolja, {Valerian V.}",

year = "1992",

month = jun,

day = "8",

doi = "10.1016/0014-5793(92)80578-5",

language = "English (US)",

volume = "304",

pages = "12--14",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

AU - Karasev, Alexander V.

AU - Kashina, Anna S.

AU - Gelfand, Vladimir I.

AU - Dolja, Valerian V.

PY - 1992/6/8

Y1 - 1992/6/8

N2 - Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603-610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 × 10-7 M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of α- and β-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.

AB - Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603-610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 × 10-7 M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of α- and β-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.

KW - Cell-to-cell movement

KW - Microtubule-associated protein

KW - Plant virus

UR - http://www.scopus.com/inward/record.url?scp=0026653019&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026653019&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(92)80578-5

DO - 10.1016/0014-5793(92)80578-5

M3 - Article

C2 - 1618294

AN - SCOPUS:0026653019

VL - 304

SP - 12

EP - 14

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -

HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this