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Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation.
RNA. 2005 Dec; 11(12):1809-24.RNA

Abstract

The cellular polypyrimidine tract-binding protein (PTB) is recruited by the genomic RNAs of picornaviruses to stimulate translation initiation at their internal ribosome entry site (IRES) elements. We investigated the contribution of the individual RNA recognition motif (RRM) domains of PTB to its interaction with the IRES of foot-and-mouth disease virus (FMDV). Using a native gel system, we found that PTB is a monomer, confirming recent reports that challenged the previous view that PTB is a dimer. Mapping the spatial orientation of PTB relative to the bound IRES RNA, we found that the two C-terminal RRM domains III and IV of PTB bind in an oriented way to the IRES. Domain III contacts the IRES stem-loop 2, while domain IV contacts the separate IRES 3' region. PTB domain I appears not to be involved directly in RNA binding, but domain II stabilizes the RNA binding conferred by domains III and IV. A PTB protein containing only these two C-terminal PTB domains is sufficient to enhance the entry of initiation factor eIF4G to the IRES and stimulate IRES activity, and the long-lived PTB-IRES interaction stabilized by domain II is not a prerequisite for this function. Thus, PTB most likely acts as an RNA chaperone to stabilize IRES structure and, in that way, augment IRES activity.

Authors+Show Affiliations

Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, 35392 Giessen, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

16314455

Citation

Song, Yutong, et al. "Evidence for an RNA Chaperone Function of Polypyrimidine Tract-binding Protein in Picornavirus Translation." RNA (New York, N.Y.), vol. 11, no. 12, 2005, pp. 1809-24.
Song Y, Tzima E, Ochs K, et al. Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. RNA. 2005;11(12):1809-24.
Song, Y., Tzima, E., Ochs, K., Bassili, G., Trusheim, H., Linder, M., Preissner, K. T., & Niepmann, M. (2005). Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. RNA (New York, N.Y.), 11(12), 1809-24.
Song Y, et al. Evidence for an RNA Chaperone Function of Polypyrimidine Tract-binding Protein in Picornavirus Translation. RNA. 2005;11(12):1809-24. PubMed PMID: 16314455.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. AU - Song,Yutong, AU - Tzima,Eleni, AU - Ochs,Kerstin, AU - Bassili,Gergis, AU - Trusheim,Heidi, AU - Linder,Monica, AU - Preissner,Klaus T, AU - Niepmann,Michael, PY - 2005/11/30/pubmed PY - 2006/1/4/medline PY - 2005/11/30/entrez SP - 1809 EP - 24 JF - RNA (New York, N.Y.) JO - RNA VL - 11 IS - 12 N2 - The cellular polypyrimidine tract-binding protein (PTB) is recruited by the genomic RNAs of picornaviruses to stimulate translation initiation at their internal ribosome entry site (IRES) elements. We investigated the contribution of the individual RNA recognition motif (RRM) domains of PTB to its interaction with the IRES of foot-and-mouth disease virus (FMDV). Using a native gel system, we found that PTB is a monomer, confirming recent reports that challenged the previous view that PTB is a dimer. Mapping the spatial orientation of PTB relative to the bound IRES RNA, we found that the two C-terminal RRM domains III and IV of PTB bind in an oriented way to the IRES. Domain III contacts the IRES stem-loop 2, while domain IV contacts the separate IRES 3' region. PTB domain I appears not to be involved directly in RNA binding, but domain II stabilizes the RNA binding conferred by domains III and IV. A PTB protein containing only these two C-terminal PTB domains is sufficient to enhance the entry of initiation factor eIF4G to the IRES and stimulate IRES activity, and the long-lived PTB-IRES interaction stabilized by domain II is not a prerequisite for this function. Thus, PTB most likely acts as an RNA chaperone to stabilize IRES structure and, in that way, augment IRES activity. SN - 1355-8382 UR - https://www.unboundmedicine.com/medline/citation/16314455/Evidence_for_an_RNA_chaperone_function_of_polypyrimidine_tract_binding_protein_in_picornavirus_translation_ L2 - http://www.rnajournal.org/cgi/pmidlookup?view=long&pmid=16314455 DB - PRIME DP - Unbound Medicine ER -