Internal initiation of mRNA translation in insect cell mediated by an internal ribosome entry site (IRES) from shrimp white spot syndrome virus (WSSV)

2006 ◽  
Vol 344 (3) ◽  
pp. 893-899 ◽  
Author(s):  
Fang Han ◽  
Xiaobo Zhang
Keyword(s):  
Internal Ribosome Entry Site ◽  
Insect Cell ◽  
White Spot Syndrome Virus ◽  
Mrna Translation ◽  
White Spot ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
White Spot Syndrome ◽  
Internal Initiation

scholarly journals Polycistronic mRNAs and internal ribosome entry site elements (IRES) are widely used by white spot syndrome virus (WSSV) structural protein genes

Virology ◽  
2009 ◽  
Vol 387 (2) ◽  
pp. 353-363 ◽  
Author(s):  
Shih-Ting Kang ◽  
Jiann-Horng Leu ◽  
Han-Ching Wang ◽  
Li-Li Chen ◽  
Guang-Hsiung Kou ◽  
...  
Keyword(s):  
Internal Ribosome Entry Site ◽  
White Spot Syndrome Virus ◽  
White Spot ◽  
Structural Protein ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
White Spot Syndrome

scholarly journals Ribonucleotide Reductase of Shrimp White Spot Syndrome Virus (WSSV): Expression and Enzymatic Activity in a Baculovirus/Insect Cell System and WSSV-Infected Shrimp

Virology ◽  
2002 ◽  
Vol 304 (2) ◽  
pp. 282-290 ◽  
Author(s):  
Shinn-Tsuen Lin ◽  
Yun-Shiang Chang ◽  
Han-Ching Wang ◽  
Huey-Fen Tzeng ◽  
Zee-Fen Chang ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Ribonucleotide Reductase ◽  
Insect Cell ◽  
White Spot Syndrome Virus ◽  
Cell System ◽  
White Spot ◽  
White Spot Syndrome

scholarly journals Internal initiation of translation from the human rhinovirus-2 internal ribosome entry site requires the binding of Unr to two distinct sites on the 5′ untranslated region

2007 ◽  
Vol 88 (11) ◽  
pp. 3043-3052 ◽  
Author(s):  
Emma C. Anderson ◽  
Sarah L. Hunt ◽  
Richard J. Jackson
Keyword(s):  
Internal Ribosome Entry Site ◽  
Binding Sites ◽  
Cold Shock ◽  
Human Rhinovirus ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Polypyrimidine Tract Binding Protein ◽  
Initiation Of Translation ◽  
Cold Shock Domain ◽  
Internal Initiation

Internal initiation of translation from the human rhinovirus-2 (HRV-2) internal ribosome entry site (IRES) is dependent upon host cell trans-acting factors. The multiple cold shock domain protein Unr and the polypyrimidine tract-binding protein have been identified as synergistic activators of HRV-2 IRES-driven translation. In order to investigate the mechanism by which Unr acts in this process, we have mapped the binding sites of Unr to two distinct secondary structure domains of the HRV-2 IRES, and have identified specific nucleotides that are involved in the binding of Unr to the IRES. The data suggest that Unr acts as an RNA chaperone to maintain a complex tertiary IRES structure required for translational competency.

scholarly journals Efficient Translation Initiation Directed by the 900-Nucleotide-Long and GC-Rich 5′ Untranslated Region of the Human Retrotransposon LINE-1 mRNA Is Strictly Cap Dependent Rather than Internal Ribosome Entry Site Mediated

2007 ◽  
Vol 27 (13) ◽  
pp. 4685-4697 ◽  
Author(s):  
Sergey E. Dmitriev ◽  
Dmitri E. Andreev ◽  
Ilya M. Terenin ◽  
Ivan A. Olovnikov ◽  
Vladimir S. Prassolov ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Internal Ribosome Entry Site ◽  
Untranslated Region ◽  
High Efficiency ◽  
Rna Binding ◽  
Cultured Cells ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Cellular Mrnas ◽  
Internal Initiation

ABSTRACT Retrotransposon L1 is a mobile genetic element of the LINE family that is extremely widespread in the mammalian genome. It encodes a dicistronic mRNA, which is exceptionally rare among eukaryotic cellular mRNAs. The extremely long and GC-rich L1 5′ untranslated region (5′UTR) directs synthesis of numerous copies of RNA-binding protein ORF1p per mRNA. One could suggest that the 5′UTR of L1 mRNA contained a powerful internal ribosome entry site (IRES) element. Using transfection of cultured cells with the polyadenylated monocistronic (L1 5′UTR-Fluc) or bicistronic (Rluc-L1 5′UTR-Fluc) RNA constructs, capped or uncapped, it has been firmly established that the 5′UTR of L1 does not contain an IRES. Uncapping reduces the initiation activity of the L1 5′UTR to that of background. Moreover, the translation is inhibited by upstream AUG codons in the 5′UTR. Nevertheless, this cap-dependent initiation activity of the L1 5′UTR was unexpectedly high and resembles that of the beta-actin 5′UTR (84 nucleotides long). Strikingly, the deletion of up to 80% of the nucleotide sequence of the L1 5′UTR, with most of its stem loops, does not significantly change its translation initiation efficiency. These data can modify current ideas on mechanisms used by 40S ribosomal subunits to cope with complex 5′UTRs and call into question the conception that every long GC-rich 5′UTR working with a high efficiency has to contain an IRES. Our data also demonstrate that the ORF2 translation initiation is not directed by internal initiation, either. It is very inefficient and presumably based on a reinitiation event.

scholarly journals A Peptide Derived from RNA Recognition Motif 2 of Human La Protein Binds to Hepatitis C Virus Internal Ribosome Entry Site, Prevents Ribosomal Assembly, and Inhibits Internal Initiation of Translation

2005 ◽  
Vol 79 (15) ◽  
pp. 9842-9853 ◽  
Author(s):  
Renuka Pudi ◽  
Sudhamani S. Ramamurthy ◽  
Saumitra Das
Keyword(s):  
Internal Ribosome Entry Site ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Recognition Motif ◽  
La Protein ◽  
Initiation Of Translation ◽  
Internal Initiation ◽  
Hcv Ires

ABSTRACT Human La protein is known to interact with hepatitis C virus (HCV) internal ribosome entry site (IRES) and stimulate translation. Previously, we demonstrated that mutations within HCV SL IV lead to reduced binding to La-RNA recognition motif 2 (RRM2) and drastically affect HCV IRES-mediated translation. Also, the binding of La protein to SL IV of HCV IRES was shown to impart conformational alterations within the RNA so as to facilitate the formation of functional initiation complex. Here, we report that a synthetic peptide, LaR2C, derived from the C terminus of La-RRM2 competes with the binding of cellular La protein to the HCV IRES and acts as a dominant negative inhibitor of internal initiation of translation of HCV RNA. The peptide binds to the HCV IRES and inhibits the functional initiation complex formation. An Huh7 cell line constitutively expressing a bicistronic RNA in which both cap-dependent and HCV IRES-mediated translation can be easily assayed has been developed. The addition of purified TAT-LaR2C recombinant polypeptide that allows direct delivery of the peptide into the cells showed reduced expression of HCV IRES activity in this cell line. The study reveals valuable insights into the role of La protein in ribosome assembly at the HCV IRES and also provides the basis for targeting ribosome-HCV IRES interaction to design potent antiviral therapy.

scholarly journals Human Cytomegalovirus Induces the Endoplasmic Reticulum Chaperone BiP through Increased Transcription and Activation of Translation by Using the BiP Internal Ribosome Entry Site

2010 ◽  
Vol 84 (21) ◽  
pp. 11479-11486 ◽  
Author(s):  
Nicholas J. Buchkovich ◽  
Yongjun Yu ◽  
Francis J. Pierciey ◽  
James C. Alwine
Keyword(s):  
Endoplasmic Reticulum ◽  
Transcriptional Activation ◽  
Internal Ribosome Entry Site ◽  
Hcmv Infection ◽  
Mrna Translation ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Unfolded Protein ◽  
Infected Cells ◽  
Protein Response

ABSTRACT The endoplasmic reticulum (ER) chaperone BiP (immunoglobulin binding protein) plays a major role in the control of the unfolded protein response. We have previously shown that BiP levels are dramatically increased during human cytomegalovirus (HCMV) infection, where BiP performs unique roles in viral assembly and egress. We show that BiP mRNA levels increase during infection due to activation of the BiP promoter by the major immediate-early (MIE) proteins. The BiP promoter, like other ER stress-activated promoters, contains endoplasmic reticulum stress elements (ERSEs), which are activated by unfolded protein response (UPR)-induced transcription factors. However, these elements are not needed for MIE protein-mediated transcriptional activation; thus, a virus-specific transcriptional activation mechanism is used. Transcriptional activation results in only a 3- to 4-fold increase in BiP mRNA, suggesting that additional mechanisms for BiP production are utilized. The BiP mRNA contains an internal ribosome entry site (IRES) which increases the level of BiP mRNA translation. We show that utilization of the BiP IRES is dramatically increased in HCMV-infected cells. Utilization of the BiP IRES can be activated by the La autoantigen, also called Sjögren's syndrome antigen B (SSB). We show that SSB/La levels are significantly increased during HCMV infection, and SSB/La depletion causes the loss of BiP IRES utilization and lowers endogenous BiP levels in infected cells. Our data show that BiP levels increase in HCMV-infected cells through the combination of increased BiP gene transcription mediated by the MIE proteins and increased BiP mRNA translation due to SSB/La-induced utilization of the BiP IRES.

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