Nucleic Acids Research, 1994, Vol. 22, No. 15 2970-2975
© 1994
ENZYMOLOGY |
Assembly of DNA polymerase 6 and e holoenzymes depends on the geometry of the DNA template
Department of Veterinary Biochemistry, University Zürich-lrchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland
*To whom correspondence should be addressed
Received May 17, 1994. Revised June 28, 1994. Accepted June 28, 1994.
To study in details the assembly of DNA polymerases 
and 
holoenzymes a circular double-stranded DNA template containing a gap of 45 nucleotides was constructed. Both replication factor C and proliferating cell nuclear antigen were absolutely required and sufficient for assembly of DNA polymerase holoenzyme complex on DNA. On such a circular DNA substrate replication protein A (or E.coli single-strand DNA binding protein) was neither required for assembly of DNA polymerase b holoenzyme complex nor for the gap-filling reaction. A circular structure of the DNA substrate was found to be absolutely critical for the ability of auxiliary proteins to interact with DNA polymerases. The linearization of the circular DNA template resulted in three dramatic effects: (i) DNA synthesis by DNA polymerase holoenzyme was abolished, (ii) the inhibition effect of replication factor C and proliferating cell nuclear antigen on DNA polymerase 
was relieved and (iii) DNA polymerase could not form anylonger a holoenzyme with replication factor C and proliferating cell nuclear antigen. The comparison of the effect of replication factor C and proliferating cell nuclear antigen on DNA polymerases , and indicated that the auxiliary proteins appear to form a mobile clamp, which can easily slide along double-stranded DNA.
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