The C-terminal zinc finger of the catalytic subunit of DNA polymerase delta is responsible for direct interaction with the B-subunit.

Journal article

DNA polymerase delta (Pol delta) plays a central role in eukaryotic chromosomal DNA replication, repair and recombination. In fission yeast, Pol delta is a tetrameric enzyme, comprising the catalytic subunit Pol3 and three smaller subunits, Cdc1, Cdc27 and Cdm1. Previous studies have demonstrated a direct interaction between Pol3 and Cdc1, the B-subunit of the complex. Here it is shown that removal of the tandem zinc finger modules located at the C-terminus of Pol3 by targeted proteolysis ren...

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Authors: Sanchez Garcia, J; Ciufo, L; Yang, X; Kearsey, S; MacNeill, SA

• Publication status: Published
• Journal: Nucleic acids research
• Volume: 32
• Issue: 10
• Pages: 3005-3016
• Publication date: 2004-01-01
• DOI: 10.1093/nar/gkh623
• EISSN: 1362-4962
• ISSN: 0305-1048
• Language: English
• Keywords: Amino Acid Sequence; Cell Cycle Proteins; Protein Binding; Catalytic Domain; Zinc Fingers; DNA Polymerase III; Fungal Proteins; Protein Subunits; Mutation; Molecular Sequence Data; Saccharomyces cerevisiae; Two-Hybrid System Techniques; Saccharomyces cerevisiae Proteins