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Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA.
Proteomics. 2008 Nov; 8(22):4782-90.P

Abstract

Initiation of translation driven by internal ribosome entry site (IRES) elements depends upon the structural organization of this mRNA region. Besides translation initiation factors (eIFs), auxiliary proteins can also affect IRES activity. With the aim to identify proteins interacting with two unrelated IRESs present in the genome of foot-and-mouth disease virus (FMDV) and hepatitis C virus (HCV) we have used a proteomic approach. This procedure allowed the identification of 21 RNA-binding proteins interacting with discrete regions of the FMDV IRES, domains 3 and 5, and 16 interacting with domain III of the HCV IRES. In support of the binding specificity, the factors interacting with domain 3 differed from those interacting with domain 5, and included three poly(rC)-binding protein (PCBP) members, besides proliferation-associated 2G4 (PA2G4) and deleted-azoospermia 1 (DAZ1) protein. Around 71% of the identified factors associated with the FMDV IRES differ from those interacting with the HCV IRES. The group of proteins interacting with the FMDV or the HCV IRES includes eIF4B and 5 subunits of eIF3, respectively, known to interact with each of these RNAs, validating the results of this approach. According to the function of the identified proteins, 55% are involved in translation control, whereas 35% play a role in different aspects of RNA lifespan. Compilation of factors preferentially associated with FMDV or HCV IRES provides a basis for examining the strategies used by IRESs to recruit the translation machinery.

Authors+Show Affiliations

Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Madrid, Spain.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18937254

Citation

Pacheco, Almudena, et al. "Riboproteomic Analysis of Polypeptides Interacting With the Internal Ribosome-entry Site Element of Foot-and-mouth Disease Viral RNA." Proteomics, vol. 8, no. 22, 2008, pp. 4782-90.
Pacheco A, Reigadas S, Martínez-Salas E. Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA. Proteomics. 2008;8(22):4782-90.
Pacheco, A., Reigadas, S., & Martínez-Salas, E. (2008). Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA. Proteomics, 8(22), 4782-90. https://doi.org/10.1002/pmic.200800338
Pacheco A, Reigadas S, Martínez-Salas E. Riboproteomic Analysis of Polypeptides Interacting With the Internal Ribosome-entry Site Element of Foot-and-mouth Disease Viral RNA. Proteomics. 2008;8(22):4782-90. PubMed PMID: 18937254.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA. AU - Pacheco,Almudena, AU - Reigadas,Sandrine, AU - Martínez-Salas,Encarnación, PY - 2008/10/22/pubmed PY - 2009/1/14/medline PY - 2008/10/22/entrez SP - 4782 EP - 90 JF - Proteomics JO - Proteomics VL - 8 IS - 22 N2 - Initiation of translation driven by internal ribosome entry site (IRES) elements depends upon the structural organization of this mRNA region. Besides translation initiation factors (eIFs), auxiliary proteins can also affect IRES activity. With the aim to identify proteins interacting with two unrelated IRESs present in the genome of foot-and-mouth disease virus (FMDV) and hepatitis C virus (HCV) we have used a proteomic approach. This procedure allowed the identification of 21 RNA-binding proteins interacting with discrete regions of the FMDV IRES, domains 3 and 5, and 16 interacting with domain III of the HCV IRES. In support of the binding specificity, the factors interacting with domain 3 differed from those interacting with domain 5, and included three poly(rC)-binding protein (PCBP) members, besides proliferation-associated 2G4 (PA2G4) and deleted-azoospermia 1 (DAZ1) protein. Around 71% of the identified factors associated with the FMDV IRES differ from those interacting with the HCV IRES. The group of proteins interacting with the FMDV or the HCV IRES includes eIF4B and 5 subunits of eIF3, respectively, known to interact with each of these RNAs, validating the results of this approach. According to the function of the identified proteins, 55% are involved in translation control, whereas 35% play a role in different aspects of RNA lifespan. Compilation of factors preferentially associated with FMDV or HCV IRES provides a basis for examining the strategies used by IRESs to recruit the translation machinery. SN - 1615-9861 UR - https://www.unboundmedicine.com/medline/citation/18937254/Riboproteomic_analysis_of_polypeptides_interacting_with_the_internal_ribosome_entry_site_element_of_foot_and_mouth_disease_viral_RNA_ L2 - https://doi.org/10.1002/pmic.200800338 DB - PRIME DP - Unbound Medicine ER -