Literature DB >> 6296442

Genetic analysis of temperature-sensitive mutants which define the gene for the major herpes simplex virus type 1 DNA-binding protein.

S K Weller, K J Lee, D J Sabourin, P A Schaffer.   

Abstract

We have assigned eight temperature-sensitive mutants of herpes simplex virus type 1 to complementation group 1-1. Members of this group fail to complement mutants in herpes simplex virus type 2 complementation group 2-2. The mutation of one member of group 1-1, tsHA1 of strain mP, has been shown to map in or near the sequence which encodes the major herpes simplex virus type 1 DNA-binding protein (Conley et al., J. Virol. 37:191-206, 1981). The mutations of five other members of group 1-1 map in or near the sequence in which the tsHA1 mutation maps, a sequence which lies near the center of UL between the genes for the viral DNA polymerase and viral glycoprotein gAgB. These mutants can be divided into two groups; the mutations of one group map between coordinates 0.385 and 0.398, and the mutations of the other group map between coordinates 0.398 and 0.413. At the nonpermissive temperature mutants in group 1-1 are viral DNA negative, and mutant-infected cells fail to react with monoclonal antibody to the 130,000-dalton DNA-binding protein. Taken together, these data indicate that mutants in complementation groups 1-1 and 2-2 define the gene for the major herpes simplex virus DNA-binding protein, an early gene product required for viral DNA synthesis.

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Year:  1983        PMID: 6296442      PMCID: PMC256417     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  46 in total

1.  DNA synthesis and DNA polymerase activity of herpes simplex virus type 1 temperature-sensitive mutants.

Authors:  G M Aron; D J Purifoy; P A Schaffer
Journal:  J Virol       Date:  1975-09       Impact factor: 5.103

2.  Qualitative complementation test for temperature-sensitive mutants of herpes simplex virus.

Authors:  C T Chu; P A Schaffer
Journal:  J Virol       Date:  1975-11       Impact factor: 5.103

3.  Herpes simplex virus proteins: DNA-binding proteins in infected cells and in the virus structure.

Authors:  G J Bayliss; H S Marsden; J Hay
Journal:  Virology       Date:  1975-11       Impact factor: 3.616

4.  Detection of specific sequences among DNA fragments separated by gel electrophoresis.

Authors:  E M Southern
Journal:  J Mol Biol       Date:  1975-11-05       Impact factor: 5.469

5.  Temperature-sensitive mutants of herpes simplex virus type 1 defective in lysis but not in transformation.

Authors:  R G Hughes; W H Munyon
Journal:  J Virol       Date:  1975-08       Impact factor: 5.103

6.  DNA-binding proteins induced by herpes simplex virus type 2 in HEp-2 cells.

Authors:  D J Purifoy; K L Powell
Journal:  J Virol       Date:  1976-08       Impact factor: 5.103

7.  Thymidine kinase activity of herpes simplex virus temperature-sensitive mutants.

Authors:  G M Aron; P A Schaffer; R J Courtney; M Benyesh-Melnick; S Kit
Journal:  Intervirology       Date:  1973       Impact factor: 1.763

8.  Proteins specified by herpes simplex virus. XI. Identification and relative molar rates of synthesis of structural and nonstructural herpes virus polypeptides in the infected cell.

Authors:  R W Honess; B Roizman
Journal:  J Virol       Date:  1973-12       Impact factor: 5.103

9.  Temperature-sensitive mutants of herpes simplex virus type 1: isolation, complementation and partial characterization.

Authors:  P A Schaffer; G M Aron; N Biswal; M Benyesh-Melnick
Journal:  Virology       Date:  1973-03       Impact factor: 3.616

10.  Amplification and characterization of a beta-globin gene synthesized in vitro.

Authors:  T Maniatis; S G Kee; A Efstratiadis; F C Kafatos
Journal:  Cell       Date:  1976-06       Impact factor: 41.582

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  98 in total

1.  Genetic evidence for multiple nuclear functions of the herpes simplex virus ICP8 DNA-binding protein.

Authors:  M Gao; D M Knipe
Journal:  J Virol       Date:  1989-12       Impact factor: 5.103

Review 2.  HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.

Authors:  A Jacobs; X O Breakefield; C Fraefel
Journal:  Neoplasia       Date:  1999-11       Impact factor: 5.715

3.  Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.

Authors:  Susan L Uprichard; David M Knipe
Journal:  J Virol       Date:  2003-07       Impact factor: 5.103

4.  Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging.

Authors:  Angela J Przech; Dong Yu; Sandra K Weller
Journal:  J Virol       Date:  2003-09       Impact factor: 5.103

5.  Surface lysine and tyrosine residues are required for interaction of the major herpes simplex virus type 1 DNA-binding protein with single-stranded DNA.

Authors:  W T Ruyechan; J W Olson
Journal:  J Virol       Date:  1992-11       Impact factor: 5.103

6.  The conserved helicase motifs of the herpes simplex virus type 1 origin-binding protein UL9 are important for function.

Authors:  R Martinez; L Shao; S K Weller
Journal:  J Virol       Date:  1992-11       Impact factor: 5.103

7.  The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization.

Authors:  G Sherman; J Gottlieb; M D Challberg
Journal:  J Virol       Date:  1992-08       Impact factor: 5.103

8.  Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein.

Authors:  D S Fierer; M D Challberg
Journal:  J Virol       Date:  1992-07       Impact factor: 5.103

9.  The influence of the herpes simplex virus-1 DNA template environment on the regulation of gene expression.

Authors:  K Leary; H H Yim; L B Zhou; R E Sekulovich; R M Sandri-Goldin
Journal:  Virus Genes       Date:  1989-09       Impact factor: 2.332

10.  The lytic cycle of Epstein-Barr virus in the nonproducer Raji line can be rescued by the expression of a 135-kilodalton protein encoded by the BALF2 open reading frame.

Authors:  G Decaussin; V Leclerc; T Ooka
Journal:  J Virol       Date:  1995-11       Impact factor: 5.103

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