DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver

Harold C. Smith; Ronald Berezney

doi:10.1016/S0006-291X(80)80041-6

DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver

Harold C. Smith
, Ronald Berezney

Biological Sciences

SUNY Buffalo

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

73 Scopus citations

Abstract

Nuclear matrices from actively replicating regenerating liver contain significant DNA polymerase α activity but only trace amounts of β polymerase. In contrast, normal liver matrices are essentially devoid of α polymerase. The matrix bound α polymerase is completely inhibited by N-ethylmaleimide and aphidocolin but not by dideoxy TTP. We propose that functional replicational complexes are assembled dynamically on the nuclear matrix during active DNA replication.

Original language	English
Pages (from-to)	1541-1547
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	97
Issue number	4
DOIs	https://doi.org/10.1016/S0006-291X(80)80041-6
State	Published - Dec 31 1980

Keywords

2′,3′ dideoxythymidine triphosphate
deoxynucleoside triphosphate(s)
dideoxy TTP
dNTP(s)
HS buffer, 2 M NaCl, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C)
LS buffer, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C)
N-ethylmaleimide
NEM
p-hydroxymercuribenzoate
PHMB

Access to Document

10.1016/S0006-291X(80)80041-6

Cite this

@article{815f6e9a2d7b44a68bf68788949ce907,

title = "DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver",

abstract = "Nuclear matrices from actively replicating regenerating liver contain significant DNA polymerase α activity but only trace amounts of β polymerase. In contrast, normal liver matrices are essentially devoid of α polymerase. The matrix bound α polymerase is completely inhibited by N-ethylmaleimide and aphidocolin but not by dideoxy TTP. We propose that functional replicational complexes are assembled dynamically on the nuclear matrix during active DNA replication.",

keywords = "2′,3′ dideoxythymidine triphosphate, deoxynucleoside triphosphate(s), dideoxy TTP, dNTP(s), HS buffer, 2 M NaCl, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C), LS buffer, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C), N-ethylmaleimide, NEM, p-hydroxymercuribenzoate, PHMB",

author = "Smith, \{Harold C.\} and Ronald Berezney",

year = "1980",

month = dec,

day = "31",

doi = "10.1016/S0006-291X(80)80041-6",

language = "English",

volume = "97",

pages = "1541--1547",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "4",

}

TY - JOUR

T1 - DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver

AU - Smith, Harold C.

AU - Berezney, Ronald

PY - 1980/12/31

Y1 - 1980/12/31

N2 - Nuclear matrices from actively replicating regenerating liver contain significant DNA polymerase α activity but only trace amounts of β polymerase. In contrast, normal liver matrices are essentially devoid of α polymerase. The matrix bound α polymerase is completely inhibited by N-ethylmaleimide and aphidocolin but not by dideoxy TTP. We propose that functional replicational complexes are assembled dynamically on the nuclear matrix during active DNA replication.

AB - Nuclear matrices from actively replicating regenerating liver contain significant DNA polymerase α activity but only trace amounts of β polymerase. In contrast, normal liver matrices are essentially devoid of α polymerase. The matrix bound α polymerase is completely inhibited by N-ethylmaleimide and aphidocolin but not by dideoxy TTP. We propose that functional replicational complexes are assembled dynamically on the nuclear matrix during active DNA replication.

KW - 2′,3′ dideoxythymidine triphosphate

KW - deoxynucleoside triphosphate(s)

KW - dideoxy TTP

KW - dNTP(s)

KW - HS buffer, 2 M NaCl, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C)

KW - LS buffer, 0.2 mM MgCl, 10 mM Tris pH 7.4 (23°C)

KW - N-ethylmaleimide

KW - NEM

KW - p-hydroxymercuribenzoate

KW - PHMB

UR - https://www.scopus.com/pages/publications/0019336880

U2 - 10.1016/S0006-291X(80)80041-6

DO - 10.1016/S0006-291X(80)80041-6

M3 - Article

C2 - 7213377

AN - SCOPUS:0019336880

SN - 0006-291X

VL - 97

SP - 1541

EP - 1547

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

DNA polymerase α is tightly bound to the nuclear matrix of actively replicating liver

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this