Characterization of a terminal deoxynucleotidyl transferase activity in mouse mammary tumor virus

R. L. Ashley, Robert Cardiff, J. S. Manning

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Mouse mammary tumor virus (MMTV) contains an enzyme which catalyzes DNA synthesis in the presence of a preformed initiator without template direction. This type of enzyme activity is characteristic of the class of polymerases called terminal deoxynucleotidyl transferase. The MMTV enzyme is localized in the viral core and its activity depends upon the presence of detergent, reducing agent, preformed initiator, and divalent cation. Optimal conditions for activity include pH 6.85 and the use of a thymidine-containing substrate and initiator. The reaction product is predominantly single stranded. Concentration-dependent inhibition by several salts is observed. Manipulation of the reaction optima and salt concentration allows the functional separation of MMTV terminal transferase activity from RNA-dependent DNA polymerase activity.

Original languageEnglish (US)
Pages (from-to)367-375
Number of pages9
JournalVirology
Volume77
Issue number1
DOIs
StatePublished - Jan 1 1977

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Mouse mammary tumor virus
DNA Nucleotidylexotransferase
Enzymes
Salts
RNA-Directed DNA Polymerase
Reducing Agents
Divalent Cations
Transferases
Detergents
Thymidine
DNA

ASJC Scopus subject areas

  • Virology

Cite this

Characterization of a terminal deoxynucleotidyl transferase activity in mouse mammary tumor virus. / Ashley, R. L.; Cardiff, Robert; Manning, J. S.

In: Virology, Vol. 77, No. 1, 01.01.1977, p. 367-375.

Research output: Contribution to journalArticle

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