Evidence map›Paper›PMID 15314153›Full record

ArticleMolecular and cellular biology2004

The B-subunit of DNA polymerase alpha-primase associates with the origin recognition complex for initiation of DNA replication.

Masashi Uchiyama, Teresa S-F Wang

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 32 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Masashi UchiyamaDepartment of Pathology, Stanford University School of Medicine, MED CTR R-272, Stanford, CA 94305-5324, USA.
Teresa S-F Wang
Stanford Medicine · US

Funding

DNA POLYMERASES IN NORMAL AND NEOPLASTIC HUMAN CELLSR01CA014835 · NCI · STANFORD UNIVERSITY · PI WANG, TERESA S · 1985 to 2006
$3.0M
NCI NIH HHS CA14835NCI NIH HHS R01 CA014835
6 · The paper itself

Abstract

The B-subunit (p70/Pol12p) of the DNA polymerase alpha-primase (Polalpha-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 Polalpha-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 Polalpha-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 Polalpha-primase in the initiation of both leading and lagging strands at the replication origins.

Indexed as

DNA ReplicationAnimalsCell CycleCell Cycle ProteinsDNA-Binding ProteinsDNA Polymerase IDNA PrimaseHumansMutationOrigin Recognition ComplexPhosphorylationProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureCell Cycle ProteinsDNA-Binding ProteinsDNA polymerase alpha-primaseDNA Polymerase IDNA PrimaseORC1 protein, humanORC1 protein, S cerevisiaeORC2 protein, humanORC2 protein, S cerevisiaeOrigin Recognition ComplexOrp2 protein, S cerevisiaeProtein SubunitsSaccharomyces cerevisiae ProteinsSpb70 protein, S cerevisiae

Identifiers

PMID15314153
PMCPMC506996
OpenAlexW1981696977

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.