Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3' exonuclease with ribonuclease H activity

The herpes simplex virus-1 DNA polymerase is a heterodimer of Mr 190,000 which consists of the products of the UL30 (Pol) and UL42 genes. The 136-kilodalton Pol gene product contains an intrinsic ribonuclease H activity that specifically degrades RNA.DNA heteroduplexes or duplex DNA substrates in th...

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Veröffentlicht in:	The Journal of biological chemistry 1989-11, Vol.264 (32), p.19266-19270
Hauptverfasser:	CRUTE, J. J, LEHMAN, I. R
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences DNA-Directed DNA Polymerase - genetics DNA-Directed DNA Polymerase - isolation & purification DNA-Directed DNA Polymerase - metabolism Endoribonucleases - metabolism Enzymes and enzyme inhibitors Exodeoxyribonuclease V Exodeoxyribonucleases - metabolism Fundamental and applied biological sciences. Psychology Kinetics Molecular Weight Ribonuclease H Simplexvirus - enzymology Simplexvirus - genetics Substrate Specificity Transferases Vero Cells
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Beschreibung
Zusammenfassung:	The herpes simplex virus-1 DNA polymerase is a heterodimer of Mr 190,000 which consists of the products of the UL30 (Pol) and UL42 genes. The 136-kilodalton Pol gene product contains an intrinsic ribonuclease H activity that specifically degrades RNA.DNA heteroduplexes or duplex DNA substrates in the 5'---3' direction. It can therefore catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during herpes DNA replication.
ISSN:	0021-9258 1083-351X