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Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs.
RNA. 1996 Dec; 2(12):1199-212.RNA

Abstract

Initiation of translation of a subset of eukaryotic mRNAs results from internal ribosomal entry. This process is exemplified by encephalomyocarditis virus (EMCV), which contains an internal ribosomal entry site (IRES) within its 5' nontranslated region that is approximately 450-nt long and consists of a series of stem-loops designated H-L. We have previously identified a cellular 58-kDa polypeptide that binds specifically to this IRES and that is implicated in its function as the pyrimidine tract-binding protein PTB. We have now mapped PTB binding sites directly on the IRES elements of EMCV and the related foot-and-mouth disease virus (FMDV) using structure-specific enzymatic probes and base-specific chemical probes. PTB bound to six sites on the EMCV IRES: site 1 (UCUU401) is upstream of domain H, site 2 is the basal helix of domain H (nt 407-410 and 440-443), site 3 (UCUUU423) is the apical loop of domain H, site 4 is the apical helix and adjacent internal bulged loop of domain K, site 5 (CUUUA750) is the apical loop of domain K, and site 6 (CCUUU815) is downstream of domain L. PTB bound to sites on the FMDV IRES that correspond precisely to EMCV sites 3, 5, and 6. These sites have the consensus sequence CUUU and form two groups that are located near to the 5' and 3' borders of these IRES elements. Their position, and the effects of mutation of them on IRES function are consistent with PTB's role in IRES-mediated initiation being to bind to multiple sites in the IRES, thereby stabilizing a specific active conformation.

Authors+Show Affiliations

A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8972770

Citation

Kolupaeva, V G., et al. "Structural Analysis of the Interaction of the Pyrimidine Tract-binding Protein With the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Foot-and-mouth Disease Virus RNAs." RNA (New York, N.Y.), vol. 2, no. 12, 1996, pp. 1199-212.
Kolupaeva VG, Hellen CU, Shatsky IN. Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs. RNA. 1996;2(12):1199-212.
Kolupaeva, V. G., Hellen, C. U., & Shatsky, I. N. (1996). Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs. RNA (New York, N.Y.), 2(12), 1199-212.
Kolupaeva VG, Hellen CU, Shatsky IN. Structural Analysis of the Interaction of the Pyrimidine Tract-binding Protein With the Internal Ribosomal Entry Site of Encephalomyocarditis Virus and Foot-and-mouth Disease Virus RNAs. RNA. 1996;2(12):1199-212. PubMed PMID: 8972770.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural analysis of the interaction of the pyrimidine tract-binding protein with the internal ribosomal entry site of encephalomyocarditis virus and foot-and-mouth disease virus RNAs. AU - Kolupaeva,V G, AU - Hellen,C U, AU - Shatsky,I N, PY - 1996/12/1/pubmed PY - 1996/12/1/medline PY - 1996/12/1/entrez SP - 1199 EP - 212 JF - RNA (New York, N.Y.) JO - RNA VL - 2 IS - 12 N2 - Initiation of translation of a subset of eukaryotic mRNAs results from internal ribosomal entry. This process is exemplified by encephalomyocarditis virus (EMCV), which contains an internal ribosomal entry site (IRES) within its 5' nontranslated region that is approximately 450-nt long and consists of a series of stem-loops designated H-L. We have previously identified a cellular 58-kDa polypeptide that binds specifically to this IRES and that is implicated in its function as the pyrimidine tract-binding protein PTB. We have now mapped PTB binding sites directly on the IRES elements of EMCV and the related foot-and-mouth disease virus (FMDV) using structure-specific enzymatic probes and base-specific chemical probes. PTB bound to six sites on the EMCV IRES: site 1 (UCUU401) is upstream of domain H, site 2 is the basal helix of domain H (nt 407-410 and 440-443), site 3 (UCUUU423) is the apical loop of domain H, site 4 is the apical helix and adjacent internal bulged loop of domain K, site 5 (CUUUA750) is the apical loop of domain K, and site 6 (CCUUU815) is downstream of domain L. PTB bound to sites on the FMDV IRES that correspond precisely to EMCV sites 3, 5, and 6. These sites have the consensus sequence CUUU and form two groups that are located near to the 5' and 3' borders of these IRES elements. Their position, and the effects of mutation of them on IRES function are consistent with PTB's role in IRES-mediated initiation being to bind to multiple sites in the IRES, thereby stabilizing a specific active conformation. SN - 1355-8382 UR - https://www.unboundmedicine.com/medline/citation/8972770/Structural_analysis_of_the_interaction_of_the_pyrimidine_tract_binding_protein_with_the_internal_ribosomal_entry_site_of_encephalomyocarditis_virus_and_foot_and_mouth_disease_virus_RNAs_ L2 - http://www.rnajournal.org/cgi/pmidlookup?view=long&pmid=8972770 DB - PRIME DP - Unbound Medicine ER -