Nucleoprotein complex formed between herpes simplex virus UL9 protein and the origin of DNA replication: inter- and intramolecular interactions.

Rabkin, Samuel D.; Hanlon, B

doi:10.1073/pnas.88.23.10946

Cited by 18 publications

(20 citation statements)

References 32 publications

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“…To date, attempts to develop an origin-directed in vitro HSV-1 DNA replication system have been unsuccessful (14,39), indicating that the seven viral replication proteins, although essential for viral DNA replication in infected cells, are insufficient for origin-driven DNA synthesis outside the cellular milieu. Therefore, as in other viral systems, cellular proteins may be required at one or more steps in HSV-1 DNA replication.…”

Section: Nf-i Is Involvedmentioning

confidence: 99%

“…Single copies of two other sequences containing OBP binding sites which are highly homologous to site I-sites II and III-are also found within oriS (Fig. 1B), while two copies of site III are found in oriL (9,15,17,19,24,29,37,39,48,49). The limits of sites I and II were defined by DNase I footprinting of partially purified OBP (17,18,25).…”

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confidence: 99%

“…These proteins include the origin-binding protein (OBP), the single-strand DNAbinding protein (ICP8), viral DNA polymerase, the polymerase accessory protein, and three proteins composing a helicaseprimase complex (reviewed in reference 7). Although necessary, these proteins are not sufficient for origin-directed DNA synthesis in that in vitro DNA replication systems that utilize only these seven proteins have not been shown to drive DNA replication (14,39).…”

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confidence: 99%

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Cellular protein interactions with herpes simplex virus type 1 oriS.

Dabrowski¹,

Carmillo²,

Schaffer³

1994

Mol. Cell. Biol.

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The herpes simplex virus type 1 (HSV-1) origin of DNA replication, oriS, contains an AT-rich region and three highly homologous sequences, sites I, II, and III, identified as binding sites for the HSV-1 origin-binding protein (OBP). In the present study, interactions between specific oriS DNA sequences and proteins in uninfected cell extracts were characterized. The formation of complexes between proteins of viral or cellular origin and DNA sequences within origins of replication has been described for a number of viral systems. Viruses in which cellular proteins have been shown or suggested to be associated with DNA replication include parvoviruses, papovaviruses, adenoviruses, and the gammaherpesvirus Epstein-Barr virus (7,32,33,36,40,46). The characterization of cellular proteins associated with DNA replication in these diverse viral groups has revealed fundamental similarities with respect to the roles these proteins play in DNA replication and mechanistic modifications particular to each group.The linear double-stranded DNA genome of herpes simplex virus type 1 (HSV-1) is 152 kb in length and encodes more than 72 unique proteins (30). Previous studies have shown that seven viral proteins are required for origin-dependent replication of the viral genome (31,38,53). These proteins include the origin-binding protein (OBP), the single-strand DNAbinding protein (ICP8), viral DNA polymerase, the polymerase accessory protein, and three proteins composing a helicaseprimase complex (reviewed in reference 7). Although necessary, these proteins are not sufficient for origin-directed DNA synthesis in that in vitro DNA replication systems that utilize only these seven proteins have not been shown to drive DNA replication (14, 39).The HSV-1 genome is composed of two covalently linked segments, the unique long and unique short segments, which are each flanked by inverted repeat sequences, the internal repeat and terminal repeats (Fig. 1A). The genome contains three origins of replication, one located with the unique long segment (oriL) and two within the repeats flanking the unique short segment (oriS) (7,41,43). oriS consists of a 90-bp sequence, including a 45-bp palindromic region (Fig. 1B), which is highly homologous to the palindromic region of the larger 144-bp oriL (27,43,51 is located an 11-bp sequence which is conserved in oriS and oriL of HSV-1 and HSV-2 as well as in oriS of a third member of the neurotropic alphaherpesvirus subfamily, varicella-zoster virus (42,44). Nine to 10 bp of this sequence are also conserved in the origins of replication of equine herpesvirus 1 and Marek's disease virus (3, 5). The 11-bp element, found once within oriS and twice in oriL, has been shown to be a high-affinity binding site for the HSV-1-specified OBP (9, 10,15,17,18,25,37,48). Single copies of two other sequences containing OBP binding sites which are highly homologous to site I-sites II and III-are also found within oriS (Fig. 1B), while two copies of site III are found in oriL (9,15,17,19,24,29,37,39,48,49). The limits o...

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Section: Nf-i Is Involvedmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Cellular protein interactions with herpes simplex virus type 1 oriS.

Dabrowski¹,

Carmillo²,

Schaffer³

1994

Mol. Cell. Biol.

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“…The Nterminal part of the protein is also necessary for efficient dimerization (Elias et al, 1992) and for the observed cooperativity in binding to ori s (Elias et al, 1990(Elias et al, , 1992Hazuda et al, 1992). Interactions involving this region probably also account for the ability of UL9 to distort and/or form complex nucleoprotein structures at the origin (Koffet aI., 1991 ;Rabkin & Hanlon, 1991 ;Fierer & Challberg, 1992).…”

Section: Introductionmentioning

confidence: 99%

A mutational analysis of the DNA-binding domain of the herpes simplex virus type 1 UL9 protein

Arbuckle¹,

Stow²

1993

Journal of General Virology

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The herpes simplex virus type 1 origin-binding protein is encoded by gene UL9. We previously described a plasmid, pB 1, which encodes a fusion protein containing only the C-terminal 317 amino acids of the UL9 polypeptide and showed that this product retains sequence-specific DNA-binding ability. Two series of pB1 mutants have now been constructed and the polypeptides were tested for origin-binding activity. Using C-terminal truncations, we show that the Cterminal 34 amino acids of UL9 are dispensable for binding and that essential residues lie between positions 801 and 818. Analysis of a series of mutants containing insertions of four amino acids at various positions identified regions of the DNA-binding domain in which alterations either abolished or had relatively little effect upon binding activity. Two mutants which were intermediate in their binding activities also exhibited temperature-or sequence-specific effects.

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“…Although the helicase assay utilizes model substrates, this finding m a y nevertheless be relevant to the way in which U L 9 functions at viral replication origins. Previous studies have indicated that sequence-specific binding of U L 9 to the viral replication origins results in the formation of higher- order nucleoprotein structures (Rabkin & Hanlon, 1991) and that distortion and wrapping of the DNA occurs under these conditions (Elias et al, 1990;Koff et al, 1991;Hazuda et al, 1992;Fierer & Challberg, 1992). The helicase-associated DNA-binding activity of UL9 molecules within the nucleoprotein complex may then allow interaction with such regions of DNA and subsequent energy-dependent unwinding of the DNA duplex.…”

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The origin-binding domain of the herpes simplex virus type 1 UL9 protein is not required for DNA helicase activity

Abbotts¹,

Stow²

1995

Journal of General Virology

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The UL9 protein of herpes simplex virus type 1 binds to specific sequences within the viral origins of DNA replication and also functions as a DNA helicase. The C-terminal 317 amino acids of the 851 residue protein specify sequence-specific binding to the viral origins and the N-terminal 400 contain several motifs characteristic of many DNA and RNA helicases. To investigate whether the origin-binding domain is required for helicase function we have expressed a truncated version comprising amino acids 1-535 of UL9 using a recombinant baculovirus. Extracts were prepared from cells infected with the recombinant virus and chromatographer over ATP-agarose. DNA helicase, DNAdependent ATPase and a novel single-stranded DNAbinding activity were present in fractions containing the truncated UL9 protein but not in corresponding gradient fractions from a control virus infection. These results indicate that the DNA helicase function of UL9 does not require the presence of the origin-binding domain and suggest that an interaction between the N-terminal domain and distorted or partially single-stranded regions of DNA may play a role in unwinding the origin region.

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Nucleoprotein complex formed between herpes simplex virus UL9 protein and the origin of DNA replication: inter- and intramolecular interactions.

Abstract: The

Cited by 18 publications

References 32 publications

Cellular protein interactions with herpes simplex virus type 1 oriS.

Cellular protein interactions with herpes simplex virus type 1 oriS.

A mutational analysis of the DNA-binding domain of the herpes simplex virus type 1 UL9 protein

The origin-binding domain of the herpes simplex virus type 1 UL9 protein is not required for DNA helicase activity

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