POL1 DNA-directed DNA polymerase alpha catalytic subunit POL1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Gene symbol: POL1
Gene description: DNA-directed DNA polymerase alpha catalytic subunit POL1
Primary source: SGD:S000005046
Locus tag: YNL102W
See related: AllianceGenome:SGD:S000005046
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: CDC17; CRT5; HPR3
Summary: Enables DNA-directed DNA polymerase activity. Involved in DNA metabolic process and premeiotic DNA replication. Located in replication fork. Part of alpha DNA polymerase:primase complex. Human ortholog(s) of this gene implicated in Van Esch-O'Driscoll syndrome and X-linked reticulate pigmentary disorder. Orthologous to human POLA1 (DNA polymerase alpha 1, catalytic subunit). [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (430087..434493)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Here the authors show that Ctf4 tightly dimerizes CMG helicase, with an extensive interface involving Psf2, Cdc45, and Sld5. Interestingly, Ctf4 binds only one Pol alpha-primase. Thus, Ctf4 may have evolved as a trimer to organize two helicases and one Pol alpha-primase into a replication factory.
Title: Ctf4 organizes sister replisomes and Pol α into a replication factory.
chromatin-derived histone complexes can be bound simultaneously by Mcm2, Pol alpha and the histone chaperone FACT that is also a replisome component.
Title: Histone H2A-H2B binding by Pol α in the eukaryotic replisome contributes to the maintenance of repressive chromatin.
ur results support a model whereby parental (H3-H4)2 complexes displaced from nucleosomes by DNA unwinding at replication forks are transferred by the CMG-Ctf4-Polalph acomplex to lagging-strand DNA for nucleosome assembly at the original location.
Title: The Mcm2-Ctf4-Polα Axis Facilitates Parental Histone H3-H4 Transfer to Lagging Strands.
Core Factor's intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location.
Title: Structural mechanism of ATP-independent transcription initiation by RNA polymerase I.
An intact Mcm10 coiled-coil interaction surface is important for origin melting, helicase assembly and the recruitment of Pol-alpha to Mcm2-7.
Title: An intact Mcm10 coiled-coil interaction surface is important for origin melting, helicase assembly and the recruitment of Pol-α to Mcm2-7.
We conclude that Fob1 and Pol I make independent contributions to establishment of silencing, though Pol I also reinforces Fob1-dependent silencing.
Title: RNA Polymerase I and Fob1 contributions to transcriptional silencing at the yeast rDNA locus.
Collectively, these data demonstrate a novel role for Ccr4-Not in Pol I transcriptional regulation that is required for bridging mTORC1 signaling to ribosomal RNA synthesis.
Title: Ccr4-not regulates RNA polymerase I transcription and couples nutrient signaling to the control of ribosomal RNA biogenesis.
Data suggest that DNA-directed DNA polymerase Pols alpha and delta are the primary lagging-strand replicases and Pol epsilon is primarily a leading-strand replicase.
Title: Heterogeneous polymerase fidelity and mismatch repair bias genome variation and composition.
Data indicate that a defective DNA polymerase alpha (Polalpha)/DNA primase/chromatin-binding protein Ctf4 complex causes unscheduled strand annealing and fork reversal.
Title: Error-free DNA damage tolerance and sister chromatid proximity during DNA replication rely on the Polα/Primase/Ctf4 Complex.
Degradation of specific nuclear proteins occurs in the cytoplasm in Saccharomyces cerevisiae
Title: Degradation of specific nuclear proteins occurs in the cytoplasm in Saccharomyces cerevisiae.

Submit: New GeneRIF Correction See all GeneRIFs (15)

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables 4 iron, 4 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA replication origin binding	IBA Inferred from Biological aspect of Ancestor more info
enables DNA-directed DNA polymerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables DNA-directed DNA polymerase activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA-directed DNA polymerase activity	IEA Inferred from Electronic Annotation more info
enables chromatin binding	IBA Inferred from Biological aspect of Ancestor more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables single-stranded DNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in DNA synthesis involved in DNA repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in RNA-templated DNA biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in double-strand break repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lagging strand elongation	IBA Inferred from Biological aspect of Ancestor more info
involved_in leading strand elongation	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitotic DNA replication initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitotic DNA replication initiation	IEA Inferred from Electronic Annotation more info
involved_in premeiotic DNA replication	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of alpha DNA polymerase:primase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of alpha DNA polymerase:primase complex	IDA Inferred from Direct Assay more info	PubMed
located_in intracellular membrane-bounded organelle	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in replication fork	IDA Inferred from Direct Assay more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: DNA-directed DNA polymerase alpha catalytic subunit POL1

NP_014297.3

EC 2.7.7.7

Catalytic subunit of the DNA polymerase I alpha-primase complex; required for the initiation of DNA replication during mitotic DNA synthesis and premeiotic DNA synthesis

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001146.8 Reference assembly

Range

430087..434493

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182940.3 → NP_014297.3 TPA: DNA-directed DNA polymerase alpha catalytic subunit POL1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014297.3

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W177, P13382

UniProtKB/TrEMBL

A0A8H4BVQ7, B3LNW1, N1NWK2

Conserved Domains (2) summary

TIGR00592
Location:29 → 1227

pol2; DNA polymerase (pol2)

pfam08996
Location:1269 → 1463

zf-DNA_Pol; DNA Polymerase alpha zinc finger