Deep-sea vent phage DNA polymerase specifically initiates DNA synthesis in the absence of primers.
Proc Natl Acad Sci U S A
; 114(12): E2310-E2318, 2017 03 21.
Article
em En
| MEDLINE
| ID: mdl-28265063
ABSTRACT
A DNA polymerase is encoded by the deep-sea vent phage NrS-1. NrS-1 has a unique genome organization containing genes that are predicted to encode a helicase and a single-stranded DNA (ssDNA)-binding protein. The gene for an unknown protein shares weak homology with the bifunctional primase-polymerases (prim-pols) from archaeal plasmids but is missing the zinc-binding domain typically found in primases. We show that this gene product has efficient DNA polymerase activity and is processive in DNA synthesis in the presence of the NrS-1 helicase and ssDNA-binding protein. Remarkably, this NrS-1 DNA polymerase initiates DNA synthesis from a specific template DNA sequence in the absence of any primer. The de novo DNA polymerase activity resides in the N-terminal domain of the protein, whereas the C-terminal domain enhances DNA binding.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bacteriófagos
/
Proteínas Virais
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DNA Viral
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DNA Polimerase Dirigida por DNA
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article