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MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3

Y Takei1, M Swietlik, A Tanoue

  • 1Wellcome/CRC Institute, Cambridge, UK. yt215@cam.ac.uk

EMBO Reports
|March 22, 2001
PubMed

Insights

We discovered MCM3AP, an enzyme that acetylates MCM3, a key protein in DNA replication. This acetylation process appears to regulate DNA replication, revealing a new regulatory pathway.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Minichromosome maintenance (MCM) proteins are crucial for initiating DNA replication.
  • MCM3 is a core component of the MCM complex, essential for DNA replication.
  • A novel MCM3-associated protein (MCM3AP) was identified.

Purpose of the Study:

  • To investigate the function of MCM3AP.
  • To determine if MCM3AP acetylates MCM3.
  • To explore the role of MCM3 acetylation in DNA replication.

Main Methods:

  • Two-hybrid screening to identify MCM3AP.
  • In vitro and in vivo acetylation assays.
  • Site-directed mutagenesis of putative acetyl-CoA binding motifs in MCM3AP.
  • Over-expression studies of MCM3AP and its mutants.

Main Results:

  • MCM3AP was identified as an acetyltransferase that specifically acetylates MCM3.
  • Chromatin-bound MCM3 is acetylated in vivo, and MCM3AP is also chromatin-bound.
  • Conserved acetyl-CoA binding motifs in MCM3AP are essential for its acetyltransferase activity.
  • Over-expression of MCM3AP inhibits DNA replication, an effect abolished by mutating the acetylase motifs.

Conclusions:

  • MCM3AP acetylates MCM3, suggesting a novel regulatory mechanism for DNA replication.
  • Acetylation of MCM3 by MCM3AP appears to play a role in regulating DNA replication.
  • This study reveals a new pathway involving MCM3 acetylation in DNA replication control.

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