TY - JOUR

T1 - RNA-protein interactions in regulation of picornavirus RNA translation

AU - Belsham, Graham J.

AU - Sonenberg, Nahum

PY - 1996/9

Y1 - 1996/9

N2 - The translation of picornavirus RNA occurs by a cap-independent, mechanism directed by a region of about 450 nucleotidase from the 5' untranslated region, termed an internal ribosome entry site (IRES). Internal initiation of protein synthesis occurs without any requirement for viral proteins. Furthermore, it is maintained when host cell protein synthesis is almost abolished. By using in vitro translation systems, two distinct families of IRES elements which have very different predicted RNA secondary structures have been defined. The cardiovirus and aphthovirus elements function poorly in this system with additional cellular proteins can stimulate translation directed by the enterovirus and rhinovirus RNAs and reduce production of aberrant initiation products. The characterization of cellular proteins interacting with the picornavirus IRES is a major focus of research. MAny different protein species can be observed to interact with regions of the IRES by in vitro analyses, e.g., UV cross-linking. However, the function and significance of many of these interactions are not known. For two proteins, La and the polypyrimidine tract-binding protein, evidence has been obtained for a functional role of their interaction with IRES elements.

AB - The translation of picornavirus RNA occurs by a cap-independent, mechanism directed by a region of about 450 nucleotidase from the 5' untranslated region, termed an internal ribosome entry site (IRES). Internal initiation of protein synthesis occurs without any requirement for viral proteins. Furthermore, it is maintained when host cell protein synthesis is almost abolished. By using in vitro translation systems, two distinct families of IRES elements which have very different predicted RNA secondary structures have been defined. The cardiovirus and aphthovirus elements function poorly in this system with additional cellular proteins can stimulate translation directed by the enterovirus and rhinovirus RNAs and reduce production of aberrant initiation products. The characterization of cellular proteins interacting with the picornavirus IRES is a major focus of research. MAny different protein species can be observed to interact with regions of the IRES by in vitro analyses, e.g., UV cross-linking. However, the function and significance of many of these interactions are not known. For two proteins, La and the polypyrimidine tract-binding protein, evidence has been obtained for a functional role of their interaction with IRES elements.

UR - http://www.scopus.com/inward/record.url?scp=0029811544&partnerID=8YFLogxK

U2 - 10.1128/mmbr.60.3.499-511.1996

DO - 10.1128/mmbr.60.3.499-511.1996

M3 - Review

C2 - 8840784

AN - SCOPUS:0029811544

VL - 60

SP - 499

EP - 511

JO - Microbiology and Molecular Biology Reviews

JF - Microbiology and Molecular Biology Reviews

SN - 1092-2172

IS - 3

ER -