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Function of the C-terminus of phi29 DNA polymerase in DNA and terminal protein binding.

Abstract：

:The thumb subdomain, located in various family B DNA polymerases in the C-terminal region, has been shown in their crystal structures to move upon binding of DNA, changing its conformation to nearly completely wrap around the DNA. It has therefore been involved in DNA binding. In agreement with this, partial proteolysis studies of phi29 DNA polymerase have shown that the accessibility of the cleavage sites located in their C-terminal region is reduced in the presence of DNA or terminal protein (TP), indicating that a conformational change occurs in this region upon substrate binding and suggesting that this region might be involved in DNA and TP binding. Therefore, we have studied the role of the C-terminus of phi29 DNA polymerase by deletion of the last 13 residues of this enzyme. This fragment includes a previously defined region conserved in family B DNA polymerases. The resulting DNA polymerase Delta13 was strongly affected in DNA binding, resulting in a distributive replication activity. Additionally, the capacity of the truncated polymerase to interact with TP was strongly reduced and its initiation activity was very low. On the other hand, its nucleotide binding affinity and its fidelity were not affected. We propose that the C-terminal 13 amino acids of phi29 DNA polymerase are involved in DNA binding and in a stable interaction with the initiator protein TP, playing an important role in the intrinsic processivity of this enzyme during polymerization.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Truniger V,Lázaro JM,Salas M

doi

10.1093/nar/gkh184

keywords:

subject

Has Abstract

pub_date

2004-01-16 00:00:00

pages

361-70

issue

1

eissn

0305-1048

issn

1362-4962

pii

32/1/361

journal_volume

32

pub_type

杂志文章

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