PT  - JOURNAL ARTICLE
AU  - Javier Fernandez-Chamorro
AU  - Rosario Francisco-Velilla
AU  - Jorge Ramajo
AU  - Encarnación Martinez-Salas
TI  - Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV IRES–driven RNA localization
AID  - 10.26508/lsa.201800131
DP  - 2019 Feb 01
TA  - Life Science Alliance
PG  - e201800131
VI  - 2
IP  - 1
4099  - https://www.life-science-alliance.org/content/2/1/e201800131.short
4100  - https://www.life-science-alliance.org/content/2/1/e201800131.full
SO  - Life Sci. Alliance2019 Feb 01; 2
AB  - Internal ribosome entry site (IRES) elements are organized in domains that guide internal initiation of translation. Here, we have combined proteomic and imaging analysis to study novel foot-and-mouth disease virus IRES interactors recognizing specific RNA structural subdomains. Besides known picornavirus IRES–binding proteins, we identified novel factors belonging to networks involved in RNA and protein transport. Among those, Rab1b and ARF5, two components of the ER-Golgi, revealed direct binding to IRES transcripts. However, whereas Rab1b stimulated IRES function, ARF5 diminished IRES activity. RNA-FISH studies revealed novel features of the IRES element. First, IRES-RNA formed clusters within the cell cytoplasm, whereas cap-RNA displayed disperse punctate distribution. Second, the IRES-driven RNA localized in close proximity with ARF5 and Rab1b, but not with the dominant-negative of Rab1b that disorganizes the Golgi. Thus, our data suggest a role for domain 3 of the IRES in RNA localization around ER-Golgi, a ribosome-rich cellular compartment.