scholarly journals Essential Role of Sna41/Cdc45 in Loading of DNA Polymerase α onto Minichromosome Maintenance Proteins in Fission Yeast

2001 ◽  
Vol 276 (28) ◽  
pp. 26189-26196 ◽  
Author(s):  
Masashi Uchiyama ◽  
Dominic Griffiths ◽  
Ken-ichi Arai ◽  
Hisao Masai
Keyword(s):  
Fission Yeast ◽  
Dna Polymerase ◽  
Essential Role ◽  
Minichromosome Maintenance ◽  
Dna Polymerase Α

Essential role of human CDT1 in DNA replication and chromatin licensing

2002 ◽  
Vol 115 (7) ◽  
pp. 1435-1440 ◽  
Author(s):  
Mickael Rialland ◽  
Francesco Sola ◽  
Corrado Santocanale
Keyword(s):  
Cell Cycle ◽  
Dna Replication ◽  
Complex Formation ◽  
Fission Yeast ◽  
Origin Recognition Complex ◽  
Essential Role ◽  
Large Body ◽  
Transformed Cells ◽  
Minichromosome Maintenance

Formation of pre-replicative complexes at origins is an early cell cycle event essential for DNA duplication. A large body of evidence supports the notion that Cdc6 protein, through its interaction with the origin recognition complex, is required for pre-replicative complex assembly by loading minichromosome maintenance proteins onto DNA. In fission yeast and Xenopus, this reaction known as the licensing of chromatin for DNA replication also requires the newly identified Cdt1 protein. We studied the role of hCdt1 protein in the duplication of the human genome by antibody microinjection experiments and analyzed its expression during the cell cycle in human non-transformed cells. We show that hCdt1 is essential for DNA replication in intact human cells, that it executes its function in a window of the cell cycle overlapping with pre-replicative complex formation and that it is necessary for the loading of minichromosome maintenance proteins onto chromatin. Intriguingly, we observed that hCdt1 protein, in contrast to other licensing factors, is already present in serum-deprived G0 arrested cells and its levels increase only marginally upon re-entry in the cell cycle.

scholarly journals Chromodomain Protein Swi6-mediated Role of DNA Polymerase α in Establishment of Silencing in Fission Yeast

2001 ◽  
Vol 276 (51) ◽  
pp. 47814-47821 ◽  
Author(s):  
Shakil Ahmed ◽  
Sharanjot Saini ◽  
Sumit Arora ◽  
Jagmohan Singh
Keyword(s):  
Fission Yeast ◽  
Dna Polymerase ◽  
Dna Polymerase Α

Role of DNA polymerase α and δ in radiation clastogenesis

1991 ◽  
Vol 262 (1) ◽  
pp. 31-36 ◽  
Author(s):  
Michael A. Bender ◽  
Ruth C. Moore ◽  
Beatrice E. Pyatt
Keyword(s):  
Dna Polymerase ◽  
Dna Polymerase Α

scholarly journals A DNA Polymerase α Accessory Protein, Mcl1, Is Required for Propagation of Centromere Structures in Fission Yeast

PLoS ONE ◽  
2008 ◽  
Vol 3 (5) ◽  
pp. e2221 ◽  
Author(s):  
Toyoaki Natsume ◽  
Yasuhiro Tsutsui ◽  
Takashi Sutani ◽  
Elaine M. Dunleavy ◽  
Alison L. Pidoux ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Dna Polymerase ◽  
Accessory Protein ◽  
Dna Polymerase Α

Regulation of the synthesis of DNA polymerase-α in regenerating liver by calcium and 1,25-dihydroxyvitamin D3

1989 ◽  
Vol 67 (7) ◽  
pp. 345-351 ◽  
Author(s):  
Marianna Sikorska ◽  
Ian de Belle ◽  
James F. Whitfield ◽  
P. Roy Walker
Keyword(s):  
Dna Polymerase ◽  
Calcium Ions ◽  
Nuclear Matrix ◽  
Critical Stage ◽  
Dihydroxyvitamin D3 ◽  
Dna Polymerase Α ◽  
Enzyme Molecules ◽  
Rat Livers ◽  
Α Activity

Digestion of nuclei from normal or partially hepatectomised rat livers with endogenous nucleases liberated a pool of cryptic DNA polymerase-α activity which had previously gone unrecognised. Most of this activity is released into the supernatant as free enzyme molecules (11S), but a small fraction of it is released as a complex of 16S (probably with DNA primase). About 40% of the enzyme remains in the pellet, which contains undigested chromatin and components of the residual nuclear matrix and nucleoskeletal structures. Virtually all of this remaining activity is extracted by 2.0 M salt. The activity of DNA polymerase-α increases equally in all nuclear fractions during the period of DNA replication in regenerating rat liver. Lowering of the serum calcium level by thyroparathyroidectomy does not affect basal DNA polymerase-α activity, but prevents induction of the enzyme during the later stages of prereplicative development. However, an injection of 1α,25-dihydroxy vitamin D3 into the rat during the first 6 h after partial hepatectomy restores the ability of the hepatocytes to induce DNA polymerase-α activity and initiate DNA synthesis. These results are discussed in terms of the role of calcium ions in the regulation of the critical stage of prereplicative development which commits the cells to DNA replication.Key words: replication, nuclear, matrix, complex, lamina, reductase.

scholarly journals The B-Subunit of DNA Polymerase α-Primase Associates with the Origin Recognition Complex for Initiation of DNA Replication

2004 ◽  
Vol 24 (17) ◽  
pp. 7419-7434 ◽  
Author(s):  
Masashi Uchiyama ◽  
Teresa S.-F. Wang
Keyword(s):  
Dna Replication ◽  
Fission Yeast ◽  
Dna Polymerase ◽  
Origin Recognition Complex ◽  
Replication Origins ◽  
Dna Polymerase Α ◽  
B Subunit ◽  
Initiation Of Dna Replication ◽  
Primase Complex ◽  
Origin Recognition

ABSTRACT The B-subunit (p70/Pol12p) of the DNA polymerase α-primase (Polα-primase) complex is thought to have a regulatory role in an early stage of S phase. We generated a panel of fission yeast thermosensitive mutants of the B-subunit (termed Spb70) to investigate its role in initiation of DNA replication by genetic and biochemical approaches. Here, we show that the fission yeast Spb70 genetically interacts and coprecipitates with origin recognition complex proteins Orp1/Orc1 and Orp2/Orc2 and primase coupling subunit Spp2/p58. A fraction of Spb70 associates with Orp2 on chromatin throughout the cell cycle independent of the other subunits of Polα-primase. Furthermore, primase Spp2/p58 subunit preferentially associates with the unphosphorylated Orp2, and the association requires Spb70. Mutations in orp2+ that abolish or mimic the Cdc2 phosphorylation of Orp2 suppress or exacerbate the thermosensitivity of the spb70 mutants, respectively, indicating that an unphosphorylated Orp2 promotes an Spb70-dependent replication event. Together, these results indicate that the chromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polα-primase complex onto replication origins in G1 pre-Start through an interaction with primase Spp2/p58 subunit. Our results thus suggest a role for the recruited Polα-primase in the initiation of both leading and lagging strands at the replication origins.

scholarly journals Role of the 2-Amino Group of Purines during dNTP Polymerization by Human DNA Polymerase α†

Biochemistry ◽  
2009 ◽  
Vol 48 (1) ◽  
pp. 180-189 ◽  
Author(s):  
Jennifer N. Patro ◽  
Milan Urban ◽  
Robert D. Kuchta
Keyword(s):  
Dna Polymerase ◽  
Amino Group ◽  
Dna Polymerase Α ◽  
Human Dna
Sign in / Sign up

Export Citation Format

Share Document