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Identification, purification, and molecular cloning of autonomously replicating sequence-binding protein 1 from

Y Murakami1, J A Huberman, J Hurwitz

  • 1Department of Viral Oncology, Institute for Virus Research, Kyoto University, Japan.

Insights

Researchers identified ARS-binding protein 1 (Abp1) in fission yeast, a protein crucial for DNA replication origins. Abp1 binds to autonomously replicating sequence (ARS) elements and shows homology to human centromere proteins, suggesting a role in linking replication and chromosome segregation.

Area of Science:

  • Molecular Biology
  • Genetics
  • Yeast Biology

Background:

  • Fission yeast autonomously replicating sequence (ARS) elements contain multiple imperfect consensus sequences.
  • These ARS elements are critical for DNA replication initiation.

Purpose of the Study:

  • To identify and characterize proteins that bind to ARS elements in Schizosaccharomyces pombe.
  • To investigate the function of a novel ARS-binding protein.

Main Methods:

  • Gel mobility-shift assays were used to detect protein-DNA complexes with ARS consensus sequences.
  • Protein purification to near homogeneity.
  • Gene cloning and sequencing of the identified ARS-binding protein.
  • Homology analysis with known proteins.

Main Results:

  • Several protein complexes bound to ARS consensus sequences and a specific origin (ars3002).
  • A 60-kDa protein, named ARS-binding protein 1 (Abp1), was purified.
  • Abp1 preferentially binds to multiple sites in ars3002 and poly[d(A.T)].
  • The Abp1 gene encodes a 59.8 kDa protein with significant homology to human/mouse centromere DNA-binding protein CENP-B.

Conclusions:

  • Abp1 is a novel protein that binds to ARS elements in S. pombe.
  • Abp1's homology to CENP-B suggests a potential role in connecting DNA replication and chromosome segregation, especially given the high density of ARS elements in S. pombe centromeres.

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