Binding of the DNA polymerase .alpha.-DNA primase complex to the nuclear matrix in HeLa cells

Biochemistry ◽  
1987 ◽  
Vol 26 (18) ◽  
pp. 5600-5607 ◽  
Author(s):  
James M. Collins ◽  
Annie K. Chu
Keyword(s):  
Dna Polymerase ◽  
Hela Cells ◽  
Nuclear Matrix ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Primase Complex

scholarly journals Eukaryotic DNA primase appears to act as oligomer in DNA-polymerase-alpha-primase complex

1992 ◽  
Vol 206 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Vladimir N. PODUST ◽  
Olga V. VLADIMIROVA ◽  
Elena N. MANAKOVA ◽  
Olga I. LAVRIK
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Eukaryotic Dna ◽  
Primase Complex

scholarly journals Conditional mutations in the yeast DNA primase genes affect different aspects of DNA metabolism and interactions in the DNA polymerase alpha-primase complex.

Genetics ◽  
1993 ◽  
Vol 133 (2) ◽  
pp. 183-191 ◽  
Author(s):  
M P Longhese ◽  
L Jovine ◽  
P Plevani ◽  
G Lucchini
Keyword(s):  
Dna Polymerase ◽  
Large Subunit ◽  
Spontaneous Mutation ◽  
Critical Role ◽  
Direct Interaction ◽  
Small Subunit ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Primase Complex

Abstract Different pri1 and pri2 conditional mutants of Saccharomyces cerevisiae altered, respectively, in the small (p48) and large (p58) subunits of DNA primase, show an enhanced rate of both mitotic intrachromosomal recombination and spontaneous mutation, to an extent which is correlated with the severity of their defects in cell growth and DNA synthesis. These effects might be attributable to the formation of nicked and gapped DNA molecules that are substrates for recombination and error-prone repair, due to defective DNA replication in the primase mutants. Furthermore, pri1 and pri2 mutations inhibit sporulation and affect spore viability, with the unsporulated mutant cells arresting with a single nucleus, suggesting that DNA primase plays a critical role during meiosis. The observation that all possible pairwise combinations of two pri1 and two pri2 alleles are lethal provides further evidence for direct interaction of the primase subunits in vivo. Immunopurification and immunoprecipitation studies on wild-type and mutant strains suggest that the small subunit has a major role in determining primase activity, whereas the large subunit directly interacts with DNA polymerase alpha, and either mediates or stabilizes association of the p48 polypeptide in the DNA polymerase alpha-primase complex.

The 68 kDa calmodulin-binding protein is tightly associated with the multiprotein DNA polymerase .alpha.-primase complex in HeLa cells

Biochemistry ◽  
1995 ◽  
Vol 34 (12) ◽  
pp. 3878-3883 ◽  
Author(s):  
Qui Ping Cao ◽  
Claire A. McGrath ◽  
Earl F. Baril ◽  
Peter J. Quesenberry ◽  
G. Prem Veer Reddy
Keyword(s):  
Dna Polymerase ◽  
Hela Cells ◽  
Binding Protein ◽  
Dna Polymerase Alpha ◽  
Calmodulin Binding ◽  
Primase Complex

scholarly journals Tight association of DNA primase with a subspecies of mouse DNA polymerase alpha.

1983 ◽  
Vol 258 (11) ◽  
pp. 6698-6700 ◽  
Author(s):  
T Yagura ◽  
S Tanaka ◽  
T Kozu ◽  
T Seno ◽  
D Korn
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Alpha ◽  
Dna Primase ◽  
Tight Association

scholarly journals DNA primase-DNA polymerase alpha from simian cells. Modulation of RNA primer synthesis by ribonucleoside triphosphates.

1985 ◽  
Vol 260 (10) ◽  
pp. 6254-6263
Author(s):  
M Yamaguchi ◽  
E A Hendrickson ◽  
M L DePamphilis
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Alpha ◽  
Dna Primase

In vitro replication of DNA containing either the SV40 or the polyoma origin

1987 ◽  
Vol 317 (1187) ◽  
pp. 439-453 ◽  
Keyword(s):  
Dna Replication ◽  
Dna Polymerase ◽  
Hela Cells ◽  
Dna Binding Protein ◽  
T Antigen ◽  
Sv40 T Antigen ◽  
Sv40 Origin ◽  
Sv40 Dna ◽  
Primase Complex

The replication of DNA containing either the polyoma or SV40 origin has been done in vitro . Each system requires its cognate large-tumour antigen (T antigen) and extracts from cells that support its replication in vivo . The host-cell source of DNA polymerase α - primase complex plays an important role in discriminating between polyoma T antigen and SV40 T antigen-dependent replication of their homologous DNA. The SV40 origin- and T antigen-dependent DNA replication has been reconstituted in vitro with purified protein components isolated from HeLa cells. In addition to SV40 T antigen, HeLa DNA polymerase α - primase complex, eukaryotic topoisomerase I and a single-strand DNA binding protein from HeLa cells are required. The latter activity, isolated solely by its ability to support SV40 DNA replication, sediments and copurifies with two major protein species of 72 and 76 kDa. Although crude fractions yielded closed circular monomer products, the purified system does not. However, the addition of crude fractions to the purified system resulted in the formation of replicative form I (RFI) products. We have separated the replication reaction with purified components into multiple steps. In an early step, T antigen in conjunction with a eukaryotic topoisomerase (or DNA gyrase) and a DNA binding protein, catalyses the conversion of a circular duplex DNA molecule containing the SV40 origin to a highly underwound covalently closed circle. This reaction requires the action of a helicase activity and the SV40 T antigen preparation contains such an activity. The T antigen associated ability to unwind DNA copurified with other activities intrinsic to T antigen (ability to support replication of SV40 DNA containing the SV40 origin, poly dT-stimulated ATPase activity and DNA helicase).

scholarly journals Subunits of the DNA polymerase alpha‐primase complex promote Notch‐mediated proliferation with discrete and shared functions in C. elegans germline

FEBS Journal ◽  
2018 ◽  
Vol 285 (14) ◽  
pp. 2590-2604 ◽  
Author(s):  
Dong Suk Yoon ◽  
Dong Seok Cha ◽  
Mohammad A. Alfhili ◽  
Brett D. Keiper ◽  
Myon‐Hee Lee
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Alpha ◽  
C Elegans ◽  
Primase Complex
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