HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr

Alexander Gragerov, Tomoshige Kino, Galina Ilyina-Gragerova, George P. Chrousos, George N. Pavlakis

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

Yeast two-hybrid selection of proteins interacting with human immunodeficiency virus type 1 Vpr identified HHR23A, a human homologue of the yeast DNA repair protein RAD23, as a specific interactor. A small 57-amino- acid C-terminal portion of HHR23A was sufficient for Vpr interaction. When introduced into human cells by transfection, full-length HHR23A or its C- terminal fragments were able to alleviate Vpr-induced cell cycle arrest, suggesting that HHR23A may participate in the pathway leading to G2 arrest by Vpr. We have also examined the effects of HHR23 on the recently identified transcription coactivator function of Vpr. The two Vpr functions are independent, since we have identified mutants lacking either the cell cycle arrest or the coactivator function. Our analysis showed that excess of HHR23A does not affect the coactivator function of Vpr, while it affects the cell cycle arresting function. Therefore, a simple sequestering model for Vpr in the presence of excess HHR23A is not supported. We propose that the interaction of HRR23A with Vpr may affect specifically pathways leading to cell cycle regulation.

Original languageEnglish
Pages (from-to)323-330
Number of pages8
JournalVirology
Volume245
Issue number2
DOIs
Publication statusPublished - 5 Jun 1998
Externally publishedYes

Fingerprint

vpr Gene Products
Fungal Proteins
Cell Cycle Checkpoints
Cell Cycle
Yeasts
DNA Repair
Transfection
HIV-1
Proteins
Amino Acids

ASJC Scopus subject areas

  • Virology

Cite this

HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr. / Gragerov, Alexander; Kino, Tomoshige; Ilyina-Gragerova, Galina; Chrousos, George P.; Pavlakis, George N.

In: Virology, Vol. 245, No. 2, 05.06.1998, p. 323-330.

Research output: Contribution to journalArticle

Gragerov, Alexander ; Kino, Tomoshige ; Ilyina-Gragerova, Galina ; Chrousos, George P. ; Pavlakis, George N. / HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr. In: Virology. 1998 ; Vol. 245, No. 2. pp. 323-330.
@article{ddf19c6ec6d2487d8f591105a7cd3824,
title = "HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr",
abstract = "Yeast two-hybrid selection of proteins interacting with human immunodeficiency virus type 1 Vpr identified HHR23A, a human homologue of the yeast DNA repair protein RAD23, as a specific interactor. A small 57-amino- acid C-terminal portion of HHR23A was sufficient for Vpr interaction. When introduced into human cells by transfection, full-length HHR23A or its C- terminal fragments were able to alleviate Vpr-induced cell cycle arrest, suggesting that HHR23A may participate in the pathway leading to G2 arrest by Vpr. We have also examined the effects of HHR23 on the recently identified transcription coactivator function of Vpr. The two Vpr functions are independent, since we have identified mutants lacking either the cell cycle arrest or the coactivator function. Our analysis showed that excess of HHR23A does not affect the coactivator function of Vpr, while it affects the cell cycle arresting function. Therefore, a simple sequestering model for Vpr in the presence of excess HHR23A is not supported. We propose that the interaction of HRR23A with Vpr may affect specifically pathways leading to cell cycle regulation.",
author = "Alexander Gragerov and Tomoshige Kino and Galina Ilyina-Gragerova and Chrousos, {George P.} and Pavlakis, {George N.}",
year = "1998",
month = "6",
day = "5",
doi = "10.1006/viro.1998.9138",
language = "English",
volume = "245",
pages = "323--330",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr

AU - Gragerov, Alexander

AU - Kino, Tomoshige

AU - Ilyina-Gragerova, Galina

AU - Chrousos, George P.

AU - Pavlakis, George N.

PY - 1998/6/5

Y1 - 1998/6/5

N2 - Yeast two-hybrid selection of proteins interacting with human immunodeficiency virus type 1 Vpr identified HHR23A, a human homologue of the yeast DNA repair protein RAD23, as a specific interactor. A small 57-amino- acid C-terminal portion of HHR23A was sufficient for Vpr interaction. When introduced into human cells by transfection, full-length HHR23A or its C- terminal fragments were able to alleviate Vpr-induced cell cycle arrest, suggesting that HHR23A may participate in the pathway leading to G2 arrest by Vpr. We have also examined the effects of HHR23 on the recently identified transcription coactivator function of Vpr. The two Vpr functions are independent, since we have identified mutants lacking either the cell cycle arrest or the coactivator function. Our analysis showed that excess of HHR23A does not affect the coactivator function of Vpr, while it affects the cell cycle arresting function. Therefore, a simple sequestering model for Vpr in the presence of excess HHR23A is not supported. We propose that the interaction of HRR23A with Vpr may affect specifically pathways leading to cell cycle regulation.

AB - Yeast two-hybrid selection of proteins interacting with human immunodeficiency virus type 1 Vpr identified HHR23A, a human homologue of the yeast DNA repair protein RAD23, as a specific interactor. A small 57-amino- acid C-terminal portion of HHR23A was sufficient for Vpr interaction. When introduced into human cells by transfection, full-length HHR23A or its C- terminal fragments were able to alleviate Vpr-induced cell cycle arrest, suggesting that HHR23A may participate in the pathway leading to G2 arrest by Vpr. We have also examined the effects of HHR23 on the recently identified transcription coactivator function of Vpr. The two Vpr functions are independent, since we have identified mutants lacking either the cell cycle arrest or the coactivator function. Our analysis showed that excess of HHR23A does not affect the coactivator function of Vpr, while it affects the cell cycle arresting function. Therefore, a simple sequestering model for Vpr in the presence of excess HHR23A is not supported. We propose that the interaction of HRR23A with Vpr may affect specifically pathways leading to cell cycle regulation.

UR - http://www.scopus.com/inward/record.url?scp=0032486250&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032486250&partnerID=8YFLogxK

U2 - 10.1006/viro.1998.9138

DO - 10.1006/viro.1998.9138

M3 - Article

VL - 245

SP - 323

EP - 330

JO - Virology

JF - Virology

SN - 0042-6822

IS - 2

ER -