Cap-binding proteins of the elF4E family are generally involved in mediating ribosome recruitment to capped mRNA via an interaction with the initiation factor elF4G. However, Schizosaccharomyces pombe has two elF4E isoforms, one of which (elF4E2, encoded by tif452) has a relatively low affinity for elF4G. We show that tif452 is required for specific stress responses. An S. pombe, tif452delta mutant manifests slow growth under conditions of nutrient, temperature and salt stress. elF4E2 shows a distinct subcellular distribution to elF4E1, the cap-binding factor that is required for mainstream translation. In response to salt stress, the cellular level of elF4E2 increases, whereas the amount of intact elF4G decreases, leaving elF4E2 as the predominant elF4E isoform in a cell deficient in ElF4G. The presence of elF4E2 modifies the competence of S. pombe ribosomes to translate mRNAs with structured leaders in vivo. The tif452 promoter has putative stress-response (T-rich) motifs, whereas elF4E2 seems to be a new type of stress-response factor.