Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits

A. John Hughes, Sharon K. Bryan, Hong Chen, Robb Moses, Charles S. McHenry

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

DNA polymerase III of Escherichia coli requires multiple auxiliary factors to enable it to serve as a replicative complex. We demonstrate that auxiliary components of the DNA polymerase III holoenzyme, the γδ complex and β subunit, markedly stimulate DNA polymerase II on long single-stranded templates. DNA polymerase II activity is enhanced by single-stranded DNA binding protein, but the stimulation by γδ and β can be observed either in the absence or presence of single-stranded DNA binding protein. In contrast with DNA polymerase III, the requirement of DNA polymerase II for γδ cannot be bypassed by large excesses of the β subunit at low ionic strength in the absence of the single-stranded DNA binding protein. The product of the DNA polymerase II-γδ-β reaction on a uniquely primed single-stranded circle is of full template length; the reconstituted enzyme apparently is incapable of strand displacement synthesis. The possible biological implications of these observations are discussed.

Original languageEnglish (US)
Pages (from-to)4568-4573
Number of pages6
JournalJournal of Biological Chemistry
Volume266
Issue number7
StatePublished - Mar 5 1991
Externally publishedYes

Fingerprint

DNA Polymerase II
DNA Polymerase III
Holoenzymes
Escherichia coli
DNA-Binding Proteins
Ionic strength
Osmolar Concentration
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits. / Hughes, A. John; Bryan, Sharon K.; Chen, Hong; Moses, Robb; McHenry, Charles S.

In: Journal of Biological Chemistry, Vol. 266, No. 7, 05.03.1991, p. 4568-4573.

Research output: Contribution to journalArticle

Hughes, A. John ; Bryan, Sharon K. ; Chen, Hong ; Moses, Robb ; McHenry, Charles S. / Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 7. pp. 4568-4573.
@article{156d8a3c70304386a21c7a9be468804c,
title = "Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits",
abstract = "DNA polymerase III of Escherichia coli requires multiple auxiliary factors to enable it to serve as a replicative complex. We demonstrate that auxiliary components of the DNA polymerase III holoenzyme, the γδ complex and β subunit, markedly stimulate DNA polymerase II on long single-stranded templates. DNA polymerase II activity is enhanced by single-stranded DNA binding protein, but the stimulation by γδ and β can be observed either in the absence or presence of single-stranded DNA binding protein. In contrast with DNA polymerase III, the requirement of DNA polymerase II for γδ cannot be bypassed by large excesses of the β subunit at low ionic strength in the absence of the single-stranded DNA binding protein. The product of the DNA polymerase II-γδ-β reaction on a uniquely primed single-stranded circle is of full template length; the reconstituted enzyme apparently is incapable of strand displacement synthesis. The possible biological implications of these observations are discussed.",
author = "Hughes, {A. John} and Bryan, {Sharon K.} and Hong Chen and Robb Moses and McHenry, {Charles S.}",
year = "1991",
month = "3",
day = "5",
language = "English (US)",
volume = "266",
pages = "4568--4573",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits

AU - Hughes, A. John

AU - Bryan, Sharon K.

AU - Chen, Hong

AU - Moses, Robb

AU - McHenry, Charles S.

PY - 1991/3/5

Y1 - 1991/3/5

N2 - DNA polymerase III of Escherichia coli requires multiple auxiliary factors to enable it to serve as a replicative complex. We demonstrate that auxiliary components of the DNA polymerase III holoenzyme, the γδ complex and β subunit, markedly stimulate DNA polymerase II on long single-stranded templates. DNA polymerase II activity is enhanced by single-stranded DNA binding protein, but the stimulation by γδ and β can be observed either in the absence or presence of single-stranded DNA binding protein. In contrast with DNA polymerase III, the requirement of DNA polymerase II for γδ cannot be bypassed by large excesses of the β subunit at low ionic strength in the absence of the single-stranded DNA binding protein. The product of the DNA polymerase II-γδ-β reaction on a uniquely primed single-stranded circle is of full template length; the reconstituted enzyme apparently is incapable of strand displacement synthesis. The possible biological implications of these observations are discussed.

AB - DNA polymerase III of Escherichia coli requires multiple auxiliary factors to enable it to serve as a replicative complex. We demonstrate that auxiliary components of the DNA polymerase III holoenzyme, the γδ complex and β subunit, markedly stimulate DNA polymerase II on long single-stranded templates. DNA polymerase II activity is enhanced by single-stranded DNA binding protein, but the stimulation by γδ and β can be observed either in the absence or presence of single-stranded DNA binding protein. In contrast with DNA polymerase III, the requirement of DNA polymerase II for γδ cannot be bypassed by large excesses of the β subunit at low ionic strength in the absence of the single-stranded DNA binding protein. The product of the DNA polymerase II-γδ-β reaction on a uniquely primed single-stranded circle is of full template length; the reconstituted enzyme apparently is incapable of strand displacement synthesis. The possible biological implications of these observations are discussed.

UR - http://www.scopus.com/inward/record.url?scp=0025847493&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025847493&partnerID=8YFLogxK

M3 - Article

C2 - 1999435

AN - SCOPUS:0025847493

VL - 266

SP - 4568

EP - 4573

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 7

ER -