Allosteric interaction of a herpes simplex viral thymidine kinase with host DNA polymerase α in mouse LP1-1 cells

C. G. Kim, Eun Shim, J. E. Lee, Y. K. Jang, C. G. Lee, S. D. Park

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A DNA polymerase α-associated multienzyme complex isolated from mouse LP1-1 cells transfected with the thymidine kinase gene of herpes simplex virus type I (1) showed activities of DNA polymerase α, topoisomerase II, and thymidine kinase (TK) in the complex. TK antiserum recognized a 43 kDa polypeptide only in the fraction of the multienzyme complex prepared from the LP1-1 cells but not that from L-M(TK-) cells. In permeabilized cells, hydroxyurea did not show any inhibitory effect on either DNA polymerase or TK, whereas aphidicolin, novobiocin and TK antiserum inhibited both enzymes. These results provide evidence for the functional association and an allosteric interaction between the viral TK and host DNA polymerase α.

Original languageEnglish (US)
Pages (from-to)651-657
Number of pages7
JournalBiochemistry and Molecular Biology International
Volume32
Issue number4
StatePublished - 1994
Externally publishedYes

Fingerprint

Herpes Simplex
Thymidine Kinase
DNA-Directed DNA Polymerase
Multienzyme Complexes
Immune Sera
DNA Polymerase II
Polynucleotide 5'-Hydroxyl-Kinase
Aphidicolin
Novobiocin
Type II DNA Topoisomerase
Hydroxyurea
Human Herpesvirus 1
Viruses
Genes
Peptides
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

Cite this

Allosteric interaction of a herpes simplex viral thymidine kinase with host DNA polymerase α in mouse LP1-1 cells. / Kim, C. G.; Shim, Eun; Lee, J. E.; Jang, Y. K.; Lee, C. G.; Park, S. D.

In: Biochemistry and Molecular Biology International, Vol. 32, No. 4, 1994, p. 651-657.

Research output: Contribution to journalArticle

Kim, C. G. ; Shim, Eun ; Lee, J. E. ; Jang, Y. K. ; Lee, C. G. ; Park, S. D. / Allosteric interaction of a herpes simplex viral thymidine kinase with host DNA polymerase α in mouse LP1-1 cells. In: Biochemistry and Molecular Biology International. 1994 ; Vol. 32, No. 4. pp. 651-657.
@article{2bc7bad66c5a4e3a9f45265f6ca34c8e,
title = "Allosteric interaction of a herpes simplex viral thymidine kinase with host DNA polymerase α in mouse LP1-1 cells",
abstract = "A DNA polymerase α-associated multienzyme complex isolated from mouse LP1-1 cells transfected with the thymidine kinase gene of herpes simplex virus type I (1) showed activities of DNA polymerase α, topoisomerase II, and thymidine kinase (TK) in the complex. TK antiserum recognized a 43 kDa polypeptide only in the fraction of the multienzyme complex prepared from the LP1-1 cells but not that from L-M(TK-) cells. In permeabilized cells, hydroxyurea did not show any inhibitory effect on either DNA polymerase or TK, whereas aphidicolin, novobiocin and TK antiserum inhibited both enzymes. These results provide evidence for the functional association and an allosteric interaction between the viral TK and host DNA polymerase α.",
author = "Kim, {C. G.} and Eun Shim and Lee, {J. E.} and Jang, {Y. K.} and Lee, {C. G.} and Park, {S. D.}",
year = "1994",
language = "English (US)",
volume = "32",
pages = "651--657",
journal = "IUBMB Life",
issn = "1521-6543",
publisher = "Wiley-Blackwell",
number = "4",

}

TY - JOUR

T1 - Allosteric interaction of a herpes simplex viral thymidine kinase with host DNA polymerase α in mouse LP1-1 cells

AU - Kim, C. G.

AU - Shim, Eun

AU - Lee, J. E.

AU - Jang, Y. K.

AU - Lee, C. G.

AU - Park, S. D.

PY - 1994

Y1 - 1994

N2 - A DNA polymerase α-associated multienzyme complex isolated from mouse LP1-1 cells transfected with the thymidine kinase gene of herpes simplex virus type I (1) showed activities of DNA polymerase α, topoisomerase II, and thymidine kinase (TK) in the complex. TK antiserum recognized a 43 kDa polypeptide only in the fraction of the multienzyme complex prepared from the LP1-1 cells but not that from L-M(TK-) cells. In permeabilized cells, hydroxyurea did not show any inhibitory effect on either DNA polymerase or TK, whereas aphidicolin, novobiocin and TK antiserum inhibited both enzymes. These results provide evidence for the functional association and an allosteric interaction between the viral TK and host DNA polymerase α.

AB - A DNA polymerase α-associated multienzyme complex isolated from mouse LP1-1 cells transfected with the thymidine kinase gene of herpes simplex virus type I (1) showed activities of DNA polymerase α, topoisomerase II, and thymidine kinase (TK) in the complex. TK antiserum recognized a 43 kDa polypeptide only in the fraction of the multienzyme complex prepared from the LP1-1 cells but not that from L-M(TK-) cells. In permeabilized cells, hydroxyurea did not show any inhibitory effect on either DNA polymerase or TK, whereas aphidicolin, novobiocin and TK antiserum inhibited both enzymes. These results provide evidence for the functional association and an allosteric interaction between the viral TK and host DNA polymerase α.

UR - http://www.scopus.com/inward/record.url?scp=0028274902&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028274902&partnerID=8YFLogxK

M3 - Article

C2 - 8038716

AN - SCOPUS:0028274902

VL - 32

SP - 651

EP - 657

JO - IUBMB Life

JF - IUBMB Life

SN - 1521-6543

IS - 4

ER -