H. Le et al., TRANSLATION INITIATION-FACTORS EIF-ISO4G AND EIF-4B INTERACT WITH THEPOLY(A)-BINDING PROTEIN AND INCREASE ITS RNA-BINDING ACTIVITY, The Journal of biological chemistry, 272(26), 1997, pp. 16247-16255
The 5'-cap and the poly(A) tail act synergistically to increase the tr
anslational efficiency of eukaryotic mRNAs, which suggests that these
two mRNA elements communicate during translation, We report here that
the cap-associated eukaryotic initiation factors (eLFs), i.e, the two
isoforms of the cap-binding complex (eIF-4F and eLF-iso4F) and eIF-4B,
bind to the poly(A)-binding protein (PABP) both in the presence and a
bsence of poly(A) RNA, The interactions between PABP and eIF-4F, eIF-i
so4F, and eIF-4B were measured in the absence of poly(A) RNA using far
Western analysis and confirmed by direct fluorescence titration studi
es, The functional consequence of the interaction between these initia
tion factors and PABP was examined using RNA binding assays and RNA mo
bility shift analysis, eIF-4F, eIF-iso4F, and eIF-4B promoted PARR act
ivity through a shift in its equilibrium affinity for poly(A), eIF-iso
4G, the large subunit of eIF-iso4F, was the subunit responsible for th
e interaction between eLF-iso4F and PABP and was the subunit that prom
oted PABP RNA binding activity, Truncation analysis of eIF-iso4G indic
ated that a domain close to its N-terminal end appeared to be involved
in binding PARR, These results suggest that the interaction between P
ABP and eIF-4B and eIF-iso4G may be involved in mediating the function
al co-dependence observed between the cap and the poly(A) tail during
translation.