Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 33, Pages 31402-31407Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M104183200
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Candida albicans EF-2 binds sordarin to a single class of binding sites with K-d = 1.26 mum. Equimolar mixtures of EF-2 and ribosomes, in the presence of a non-hydrolyzable GTP analog, reveal two classes of high affinity sordarin binding sites with K-d = 0.7 and 41.5 nm, probably due to the existence of two ribosome populations. Photoaffinity labeling of C. albicans EF-2 in the absence of ribosomes has been performed with [C-14]GM258383, a photoactivatable sordarin derivative. Labeling is saturable and can be considered specific, because it can be prevented with another sordarin analog. The fragment GIn(224)-LYS232 has been identified as the modified peptide within the EF-2 sequence, Lys(228) being the residue to which the photoprobe was linked. This fragment is included within the G -subdomain of EF-2. These results are discussed in the light of the high sordarin specificity toward fungal systems.
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