TY - JOUR
T1 - Post-transcriptional processing of cellular RNAs in herpes simplex virus-infected cells
AU - Taddeo, B.
AU - Esclatine, A.
AU - Roizman, B.
PY - 2004/11
Y1 - 2004/11
N2 - In HSV-1 (herpes simplex virus 1)-infected cells, the UL41 gene product carried with the virion has been shown to mediate the degradation of mRNA, leading to the shut-off of cellular protein synthesis. Analysis of the RNAs accumulating in cells infected with HSV-1 revealed the accumulation of RNAs encoding numerous cellular proteins both associated with and independent of activation of the NF-κB (nuclear factor κB) pathway. Studies on the activation of NF-κK and the expression and fate of selected cellular transcripts revealed the following, (i) In HSV-1-infected cells, NF-κB is activated by activated protein kinase R. Furthermore, the blockade of NF-κB translocation by suppression of protein kinase R activation does not render the cell more susceptible to apoptosis induced by viral gene expression. (ii) A number of mRNA up-regulated in infected cells [e.g. IκBα (inhibitory κBα), the immediate-early response protein IEX-1 and c-fos] are partially degraded and not translated. The degradation is U L41-dependent and results in deadenylation, endonucleolytic cleavage and 3′-5′ degradation. The 5′-portion resulting from the endonucleolytic cleavage tends to linger in the infected cells. To date, the RNAs processed in this manner contained ARE (AU-rich elements) in their 3′-untranslated domains. RNAs lacking ARE were expressed and not degraded in this manner. (iii) Tristetraprolin and T-cell internal antigen-1, cellular proteins involved in the degradation of ARE-containing RNAs, are induced and activated in infected cells and tristetraprolin interacts physically with the UL41 protein.
AB - In HSV-1 (herpes simplex virus 1)-infected cells, the UL41 gene product carried with the virion has been shown to mediate the degradation of mRNA, leading to the shut-off of cellular protein synthesis. Analysis of the RNAs accumulating in cells infected with HSV-1 revealed the accumulation of RNAs encoding numerous cellular proteins both associated with and independent of activation of the NF-κB (nuclear factor κB) pathway. Studies on the activation of NF-κK and the expression and fate of selected cellular transcripts revealed the following, (i) In HSV-1-infected cells, NF-κB is activated by activated protein kinase R. Furthermore, the blockade of NF-κB translocation by suppression of protein kinase R activation does not render the cell more susceptible to apoptosis induced by viral gene expression. (ii) A number of mRNA up-regulated in infected cells [e.g. IκBα (inhibitory κBα), the immediate-early response protein IEX-1 and c-fos] are partially degraded and not translated. The degradation is U L41-dependent and results in deadenylation, endonucleolytic cleavage and 3′-5′ degradation. The 5′-portion resulting from the endonucleolytic cleavage tends to linger in the infected cells. To date, the RNAs processed in this manner contained ARE (AU-rich elements) in their 3′-untranslated domains. RNAs lacking ARE were expressed and not degraded in this manner. (iii) Tristetraprolin and T-cell internal antigen-1, cellular proteins involved in the degradation of ARE-containing RNAs, are induced and activated in infected cells and tristetraprolin interacts physically with the UL41 protein.
KW - AU-rich element
KW - Herpes simplex virus type 1 (HSV-1)
KW - Microarray
KW - Nuclear factor-κB
KW - RNA turnover [email protected]
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U2 - 10.1042/BST0320697
DO - 10.1042/BST0320697
M3 - Article
C2 - 15493991
AN - SCOPUS:8744299600
SN - 0300-5127
VL - 32
SP - 697
EP - 701
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
IS - 5
ER -