Structures of herpes simplex virus type 1 genes required for replication of virus DNA

McGeoch, Duncan J.; Dalrymple, M A; Dolan, Aidan; McNab, David; Perry, Lise J.; Taylor, Philip L.; Challberg, Mark D.

doi:10.1128/jvi.62.2.444-453.1988

Cited by 151 publications

(91 citation statements)

References 51 publications

(54 reference statements)

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“…The first clue towards the DNA binding property of the protein was from a small but provocative region of amino acid sequence similar to that of a DNA binding protein (UL 42) from herpes simplex virus (50). In vitro DNA binding assays with the purified protein confirmed the DNA binding ability of E. coli-Dps.…”

Section: Dna Binding Propertymentioning

confidence: 95%

Stress Responses in Mycobacteria

Gupta

Chatterji

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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SummaryMycobacterium tuberculosis is a successful pathogen that overcomes numerous challenges presented by the immune system of the host. This bacterium usually establishes a chronic infection in the host where it may silently persist inside a granuloma until, a failure in host defenses, leads to manifestation of the disease. None of the conventional anti-tuberculosis drugs are able to target these persisting bacilli. Development of drugs against such persisting bacilli is a constant challenge since the physiology of these dormant bacteria is still not understood at the molecular level. Some evidence suggests that the in vivo environment encountered by the persisting bacteria is anoxic and nutritionally starved. Based on these assumptions, anaerobic and starved cultures are used as models to study the molecular basis of dormancy. This review outlines the problem of persistence of M. tuberculosis and the various in vitro models used to study mycobacterial latency. The basis of selecting the nutritional starvation model has been outlined here. Also, the choice of M. smegmatis as a model suitable for studying mycobacterial latency is discussed. Lastly, general issues related to oxidative stress and bacterial responses to it have been elaborated. We have also discussed general control of OxyR-mediated regulation and emphasized the processes which manifest in the absence of functional OxyR in the bacteria. Lastly, a new class of protein called Dps has been reviewed for its important role in protecting DNA under stress. IUBMB Life, 57: 149 -159, 2005

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Section: Dna Binding Propertymentioning

confidence: 95%

Stress Responses in Mycobacteria

Gupta

Chatterji

2005

IUBMB Life (International Union of Biochemistry and Molecular B

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“…Plasmid probes were constructed by standard methods (18). The sequence of the Hindlll L fragment of HSV-1 strain 17 was kindly provided by Duncan McGeoch (22,23). The plasmid pGX80, containing the Hindlll L fragment, was produced by B. Matz and used to obtain subclones specific for 65KDBp and glycoprotein C (gC).…”

Section: Methodsmentioning

confidence: 99%

“…The plasmid pGX80, containing the Hindlll L fragment, was produced by B. Matz and used to obtain subclones specific for 65KDBp and glycoprotein C (gC). Plasmid pLPS19A contained a 738-base-pair PstI fragment located entirely within the 65KDBP open reading frame (23), cloned into the PstI site of the multifunctional cloning vector pTZ19U (United States Biochemical Corp., Cleveland, Ohio). Plasmid pgC-EX was constructed by cloning the 918-base-pair EcoRI-to-Xbal fragment located within the open reading frame encoding gC (8) into the multiple cloning site of pTZ18U.…”

Section: Methodsmentioning

confidence: 99%

Kinetics of expression of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1

Goodrich

Rixon

Parris

1989

J Virol

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The 65-kilodalton DNA-binding protein (65KDBp) of herpes simplex virus type 1, encoded by gene UL42, is required for herpes simplex virus origin-dependent DNA replication (C. A. Wu, N. J. Nelson, D. J. McGeoch, and M. D. Challberg, J. Virol. 62:435-443, 1988). We found by indirect immunofluorescence with monoclonal antibody to 65KDBP that the protein was first detectable at 3 h postinfection. It localized first to the inner periphery of the nucleus, but accumulated in large globular compartments within the nucleus by 6 h postinfection in a pattern similar to that displayed by the major DNA-binding protein ICP8. Immune electron microscopy revealed that 65KDBP was associated with the marginated heterochromatin at the early times, but migrated further into the nucleus at late times when the only discernible areas devoid of 65KDBP were the nucleoli and heterochromatin. The 65KDBP gene is a member of the 0i kinetic class as determined by the ability of the mRNA to be expressed at significant levels even in the absence of viral DNA synthesis. Furthermore, in the presence or absence of the DNA polymerase inhibitor phosphonoacetic acid, the patterns of accumulation of protein as well as mRNA were virtually indistinguishable from those displayed by the model 0 genes encoding ICP8 and thymidine kinase. Nuclear run-on experiments demonstrated that maximum rates of

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“…The HSV-1 genome encodes seven proteins that are required for origin-dependent DNA replication. They consist of a DNA polymerase and its accessory protein, a heterotrimeric helicase-primase, a single-strand (ss) DNA-binding protein and an originbinding protein, termed UL9 (Elias et al, 1986;McGeoch et al, 1988;Wu et al, 1988;Challberg and Kelly, 1989;Crute et al, 1989). Key to understanding the early events in HSV-1 replication as in other systems is learning how UL9 protein interacts with the HSV-1 origins of replication and how it may alter the structure of the DNA at the origin.…”

Section: Introductionmentioning

confidence: 99%

The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structures.

et al. 1996

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The UL9 protein of herpes simplex virus type 1 (HSV‐1) binds specifically to the HSV‐1 oriS and oriL origins of replication, and is a DNA helicase and DNA‐dependent NTPase. In this study electron microscopy was used to investigate the binding of UL9 protein to DNA fragments containing oriS. In the absence of ATP, UL9 protein was observed to bind specifically to oriS as a dimer or pair of dimers, which bent the DNA by 35 degrees +/− 15 degrees and 86 degrees +/− 38 degrees respectively, and the DNA was deduced to make a straight line path through the protein complex. In the presence of 4 mM ATP, binding at oriS was enhanced 2‐fold, DNA loops or stem‐loops were extruded from the UL9 protein complex at oriS, and the DNA in them frequently appeared highly condensed into a tight rod. The stem‐loops contained from a few hundred to over one thousand base pairs of DNA and in most, oriS was located at their apex, although in some, oriS was at a border. The DNA in the stem‐loops could be stabilized by photocrosslinking, and when Escherichia coli SSB protein was added to the incubations, it bound the stem‐loops strongly. Thus the DNA strands in the stem‐loops exist in a partially paired, partially single‐stranded state presumably making them available for ICP8 binding in vivo. These observations provide direct evidence for an origin specific unwinding by the HSV‐1 UL9 protein and for the formation of a relatively stable four‐stranded DNA in this process.

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Structures of herpes simplex virus type 1 genes required for replication of virus DNA

Cited by 151 publications

References 51 publications

Stress Responses in Mycobacteria

Stress Responses in Mycobacteria

Kinetics of expression of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1

The herpes simplex virus type 1 origin-binding protein carries out origin specific DNA unwinding and forms stem-loop structures.

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