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The mutant, designated Z1-2D Etar, did not utilize di- and tripeptides containing leucine or lysine although it contained peptidases which released the required amino acids from these substrates. S. cerevisiae Z1-2D Etar did not accumulate radioactivity from [14C]glycyl-L-leucine under conditions identical to those in which the parent took up the label from this dipeptide. These results indicate that the mutant lacks the cellular mechanism to transport peptides to the site of the peptidase activity and that di- and tripeptides share a common mode of entry into yeast.<\/jats:p>","DOI":"10.1128\/jb.136.3.1174-1177.1978","type":"journal-article","created":{"date-parts":[[2020,1,3]],"date-time":"2020-01-03T16:27:59Z","timestamp":1578068879000},"page":"1174-1177","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":8,"title":["Isolation of a peptide transport-deficient mutant of yeast"],"prefix":"10.1128","volume":"136","author":[{"given":"R","family":"Marder","sequence":"first","affiliation":[]},{"given":"B","family":"Rose","sequence":"additional","affiliation":[]},{"given":"J M","family":"Becker","sequence":"additional","affiliation":[]},{"given":"F","family":"Naider","sequence":"additional","affiliation":[]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1073\/pnas.70.2.456","article-title":"Illicit transport: the oligopeptide permease","volume":"70","author":"Ames B. 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