The Cowbird (M. Ater) and the Cuckoo (C. Canorus)

Preston, F. W.

doi:10.2307/1930349

Cited by 52 publications

(69 citation statements)

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“…The TK gene can code for a protein containing 376 amino acids with a molecular weight of 40,900. This also compares favorably with the estimated molecular weight of 40,000-44,000 obtained from NaDodSOjpolyacrylamide gel electrophoresis, (2)(3)(4)30 Table 2 indicates the number of times each codon is used and the overall amino acid composition. While all but four codons are used at least once, the distribution of codon usage is somewhat unusual.…”

Section: Methodssupporting

confidence: 58%

“…The TK gene is an early gene of HSV. In a lytic infection, expression of at least one immediate-early gene of the virus is necessary before expression of the TK gene can occur, and some product of the late genes of the virus (those expressed after the onset of viral DNA synthesis) results in the shutoff of TK gene expression (4,5). This regulatory effect is believed to occur at the transcriptional level (4,5).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Nucleotide sequence of the thymidine kinase gene of herpes simplex virus type 1.

Wagner¹,

Sharp²,

Summers³

1981

Proc. Natl. Acad. Sci. U.S.A.

344

194

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Section: Methodssupporting

confidence: 58%

mentioning

confidence: 99%

Nucleotide sequence of the thymidine kinase gene of herpes simplex virus type 1.

Wagner¹,

Sharp²,

Summers³

1981

Proc. Natl. Acad. Sci. U.S.A.

344

194

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“…[3][4][5]. Although not essential for viral replication, ICP0 increases the probability of the virus entering lytic infection, particularly after low multiplicity infection of human fibroblasts, and in its absence, viral genomes are more likely to become repressed and establish a quiescent infection (5)(6)(7). ICP0 stimulates the expression of all three classes of viral genes by as yet uncertain mechanisms that correlate with its ability to induce the degradation of a number of cellular proteins (8 -12).…”

mentioning

confidence: 99%

A RING Finger Ubiquitin Ligase Is Protected from Autocatalyzed Ubiquitination and Degradation by Binding to Ubiquitin-specific Protease USP7

Canning

Boutell

Parkinson

et al. 2004

Journal of Biological Chemistry

127

122

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Herpes simplex virus type 1 immediate-early regulatory protein ICP0 stimulates lytic infection and reactivation from latency, processes that require the ubiquitin E3 ligase activity mediated by the RING finger domain in the N-terminal portion of the protein. ICP0 stimulates the production of polyubiquitin chains by the ubiquitin-conjugating enzymes UbcH5a and UbcH6 in vitro, and in infected and transfected cells it induces the proteasome-dependent degradation of a number of cellular proteins including PML, the major constituent protein of PML nuclear bodies. However, ICP0 binds strongly to the cellular ubiquitin-specific protease USP7, a member of a family of proteins that cleave polyubiquitin chains and/or ubiquitin precursors. The region of ICP0 that is required for its interaction with USP7 has been mapped, and mutations in this domain reduce the functionality of ICP0. These findings pose the question: why does ICP0 include domains that are associated with the potentially antagonistic functions of ubiquitin conjugation and deconjugation? Here we report that although neither protein affected the intrinsic activities of the other in vitro, USP7 protected ICP0 from autoubiquitination in vitro, and their interaction can greatly increase the stability of ICP0 in vivo. These results demonstrate that RING finger-mediated autoubiquitination of ICP0 is biologically relevant and can be regulated by interaction with USP7. This principle may extend to a number of cellular RING finger E3 ubiquitin ligase proteins that have analogous interactions with ubiquitin-specific cleavage enzymes.Herpes simplex virus type 1 (HSV-1) 1 is a common human pathogen that can establish a lifelong quiescent infection in sensory neurons following primary infection of epithelial cells. Environmental stimuli such as stress and sunlight trigger periodic recurrences of lytic infection, causing cold sores and genital lesions. HSV-1 expresses three broad groups of temporally regulated genes during lytic infection, termed immediate-early (IE), early, and late (for reviews, see Refs. 1 and 2). The IE protein ICP0 has an important role in the mechanisms that govern the switch between lytic and latent infection (reviewed in Refs. 3-5). Although not essential for viral replication, ICP0 increases the probability of the virus entering lytic infection, particularly after low multiplicity infection of human fibroblasts, and in its absence, viral genomes are more likely to become repressed and establish a quiescent infection (5-7). ICP0 stimulates the expression of all three classes of viral genes by as yet uncertain mechanisms that correlate with its ability to induce the degradation of a number of cellular proteins (8 -12). ICP0 includes a zinc-binding RING finger domain in its N-terminal portion, and in its C-terminal third lie a nuclear localization signal and motifs required for self-multimerization and efficient localization at specific nuclear substructures known as ND10 or PML nuclear bodies. Consistent with its ability to induce the degradation of...

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“…The aICP4 protein appears to exert positive and negative effects on HSV gene expression. At the nonpermissive temperature (NPT), temperature-sensitive mutants defective in ICP4 overproduce a mRNAs and proteins but fail to induce the expression of/3, 'yi, and y2 mRNAs and proteins (9)(10)(11)(12)(13). The aICP4 and aICPO proteins can induce the expression of ,B genes introduced into cells by transfection (14)(15)(16)), but it is not known if ICPO is involved in the induction of HSV gene expression during a lytic infection.…”

mentioning

confidence: 99%

Transcriptional control of herpesvirus gene expression: gene functions required for positive and negative regulation.

Godowski¹,

Knipe²

1986

Proc. Natl. Acad. Sci. U.S.A.

157

160

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We have used an in vitro nuclear run-off assay to measure the levels of transcription of specific herpes simplex virus genes at different times during a lytic infection. We analyzed the effects of inhibition of DNA replication and of defects in two herpes simplex virus regulatory proteins on the transcription of these genes. We present evidence that the transcription of the aJCP4 gene is negatively regulated during a lytic infection. The regulation of ICP4 gene transcription requires the fi protein ICP8 (where ICP = infected cell polypeptide). Transcription of the PICP8, yICP5, and y2 glycoprotein C (gC) genes was dependent on ICP4, and transcription of the y2gC gene was strongly inhibited when DNA replication was blocked. Defects in ICP8 also resulted in increased levels of transcription of the ICP4, ICP8, ICP5, and gC genes from parental viral genomes. Our results suggest that ICP8 may be important in maintaining the highly ordered cascade of viral gene expression. 256The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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The Cowbird (M. Ater) and the Cuckoo (C. Canorus)

Cited by 52 publications

References 0 publications

Nucleotide sequence of the thymidine kinase gene of herpes simplex virus type 1.

Nucleotide sequence of the thymidine kinase gene of herpes simplex virus type 1.

A RING Finger Ubiquitin Ligase Is Protected from Autocatalyzed Ubiquitination and Degradation by Binding to Ubiquitin-specific Protease USP7

Transcriptional control of herpesvirus gene expression: gene functions required for positive and negative regulation.

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