Document Detail


Processing of alpha-globin and ICP0 mRNA in cells infected with herpes simplex virus type 1 ICP27 mutants.
MedLine Citation:
PMID:  10906184     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Herpes simplex virus (HSV) ICP27 is an essential and multifunctional regulator of viral gene expression that modulates RNA splicing, polyadenylation, and nuclear export. We have previously reported that ICP27 causes the cytoplasmic accumulation of unspliced alpha-globin pre-mRNA. Here we examined the effects of a series of ICP27 mutations that alter important functional regions of the protein on the processing and nuclear transport of alpha-globin and HSV ICP0 RNA. The results demonstrate that ICP27 mutants that are impaired for growth in noncomplementing cells, including mutants in the N- and C-terminal regions, are defective in the accumulation of alpha-globin pre-mRNA. Unexpectedly, several mutants that are competent to repress the expression of reporter genes in transient transfection assays failed to accumulate unspliced RNA, implying that different mechanisms are responsible for transrepression and pre-mRNA accumulation. Several mutants caused a marked increase in the length and heterogeneity of the alpha-globin mRNA poly(A) tail, suggesting that ICP27 may directly or indirectly affect the regulation of poly(A) polymerase. ICP27 was also required for the accumulation of multiple ICP0 intron-bearing transcripts, but this effect displayed a mutational sensitivity profile different from that of accumulation of unspliced alpha-globin RNA. Moreover, unlike spliced and unspliced alpha-globin RNAs, which were efficiently exported to the cytoplasm, spliced and intron-containing ICP0 transcripts were predominantly nuclear in localization, and ICP27 was not required for nuclear retention of the spliced message. We propose that these transcript- and ICP27 allele-specific differences may be explained by the presence of a strong cis-acting ICP27 response element in the alpha-globin transcript.
Authors:
K S Ellison; S A Rice; R Verity; J R Smiley
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  74     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  2000 Aug 
Date Detail:
Created Date:  2000-08-18     Completed Date:  2000-08-18     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  7307-19     Citation Subset:  IM    
Affiliation:
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
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MeSH Terms
Descriptor/Qualifier:
Globins / genetics*,  metabolism
HeLa Cells / virology
Herpesvirus 1, Human / genetics*,  metabolism
Humans
Immediate-Early Proteins / genetics*,  metabolism,  physiology*
Introns / genetics
Mutation
Poly A
RNA Processing, Post-Transcriptional*
RNA Splicing
RNA, Messenger / genetics,  metabolism*
RNA, Viral / genetics,  metabolism
Subcellular Fractions
Transcription, Genetic
Ubiquitin-Protein Ligases
Virus Replication
Grant Support
ID/Acronym/Agency:
AI42737/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/ICP27 protein, human herpesvirus 1; 0/Immediate-Early Proteins; 0/RNA, Messenger; 0/RNA, Viral; 24937-83-5/Poly A; 9004-22-2/Globins; EC 6.3.2.19/Ubiquitin-Protein Ligases; EC 6.3.2.19/Vmw110 protein, Human herpesvirus 1
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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