DNA primase associated with 10 S DNA polymerase α from calf thymus

1983 ◽  
Vol 741 (3) ◽  
pp. 348-357 ◽  
Author(s):  
Shonen Yoshida ◽  
Rika Suzuki ◽  
Shigeo Masaki ◽  
Osamu Koiwai
Keyword(s):  
Dna Polymerase ◽  
Dna Primase ◽  
Dna Polymerase Α ◽  
Calf Thymus

Structural study of immunoaffinity-purified DNA polymerase α-DNA primase complex from calf thymus

1988 ◽  
Vol 950 (3) ◽  
pp. 263-273 ◽  
Author(s):  
Katsuyuki Tamai ◽  
Kiyohide Kojima ◽  
Takamasa Hanaichi ◽  
Shigeo Masaki ◽  
Motoshi Suzuki ◽  
...  
Keyword(s):  
Structural Study ◽  
Dna Polymerase ◽  
Dna Primase ◽  
Dna Polymerase Α ◽  
Calf Thymus ◽  
Primase Complex

scholarly journals Interactions of calf thymus DNA polymerase α with primer/templates

1995 ◽  
Vol 23 (20) ◽  
pp. 4109-4115 ◽  
Author(s):  
Harry C. Thompson ◽  
Robert J. Sheaff ◽  
Robert D. Kuchta
Keyword(s):  
Dna Polymerase ◽  
Calf Thymus Dna ◽  
Dna Polymerase Α ◽  
Calf Thymus

Stimulation of Calf Thymus DNA Polymerase α Activity by Nucleolar Protein B23

1994 ◽  
Vol 199 (1) ◽  
pp. 46-51 ◽  
Author(s):  
M. Takemura ◽  
N. Ohta ◽  
Y. Furuichi ◽  
T. Takahashi ◽  
S. Yoshida ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Nucleolar Protein ◽  
Calf Thymus Dna ◽  
Dna Polymerase Α ◽  
Calf Thymus ◽  
Protein B23 ◽  
Α Activity ◽  
Stimulation Of

DNA polymerase α-DNA primase from human lymphoblasts

1988 ◽  
Vol 951 (2-3) ◽  
pp. 290-297 ◽  
Author(s):  
Gabriele Bialek ◽  
Heinz-Peter Nasheuer ◽  
Hilde Goetz ◽  
Barbara Behnke ◽  
Frank Grosse
Keyword(s):  
Dna Polymerase ◽  
Dna Primase ◽  
Dna Polymerase Α

Mammalian DNA polymerase α : a replication-competent holoenzyme form from calf thymus

1987 ◽  
Vol 317 (1187) ◽  
pp. 421-428 ◽  
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Consensus Sequence ◽  
Porcine Circovirus ◽  
Chromosomal Replication ◽  
Dna Polymerase Α ◽  
Calf Thymus ◽  
Dna Replication Origins ◽  
Cellular Dna

Calf thymus DNA polymerase α, like the replication-specific DNA polymerase III holoenzyme of Escherichia coli , can be isolated as a distinct complex. A specific multiprotein form of the polymerase α, a form designated replication-com petent (RC) holoenzyme, consists of a complex of a polymerase-primase core and at least six other polypeptides. The RC holoenzyme can efficiently replicate several naturally occurring templates, including the genomic DNA of the porcine circovirus (PCV). The DNA of this virion consists of a single-stranded circle with a defined replication origin, and its replication requires the cellular DNA replication machinery. It might therefore provide an invaluable opportunity to investigate chromosomal replication mechanisms, analogous to the way that studies on E. coli bacteriophage DNA replication elucidated host DNA replication mechanisms. Calf RC holoenzyme α selectively initiates pcv DNA replication in vitro at a site that possibly represents a consensus sequence of cellular DNA replication origins. The cell-free PCV replication system will be exploited for the in vitro dissection and reconstitution of the RC holoenzyme and the functional analysis of its component polypeptides.

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