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Figure 2 | SpringerPlus

Figure 2

From: The ClpS-like N-domain is essential for the functioning of Ubr11, an N-recognin in Schizosaccharomyces pombe

Figure 2

Uptake of dipeptides by the ubr11 mutants. A host strain (ubr11โˆ† leu1 ura4) was transformed with ura4+ plasmids encoding Ubr11 mutant or wild type proteins. Their ability to rescue the growth defect of the leucine auxotrophic host strain in the presence of leucine-containing dipeptides was tested. Serially diluted cells were spotted on the medium containing the indicated peptides or leucine. The control medium lacked any source of leucine. The ubr11-T1 mutation, which impaired recognition of type 1 residues, did not affect the utilization of the dipeptides. In contrast, the type 2-specific ubr11-T2 mutant was mostly defective.

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