Pub. Date : 2014 Nov
PMID : 25172766
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The peptide transporter Ptr2 plays a central role in di- or tripeptide import in Saccharomyces cerevisiae. | tripeptide K-26 | Ptr2p | Saccharomyces cerevisiae S288C |
| 2 | Expression of Ptr2 carrying one of the 14 mutations of which the corresponding residues of PepTst are involved in peptide recognition, salt bridge interaction, or peptide translocation failed to enable ptr2Deltatrp1 cell growth in alanyl-tryptophan (Ala-Trp) medium. | L-Alanyl-L-tryptophan | Ptr2p | Saccharomyces cerevisiae S288C |
| 3 | We observed that Ptr2 underwent rapid degradation after cycloheximide treatment (half-life, approximately 1 h), and this degradation depended on Rsp5 ubiquitin ligase. | Cycloheximide | Ptr2p | Saccharomyces cerevisiae S288C |
| 4 | The ubiquitination of Ptr2 most likely occurs at the N-terminal lysines 16, 27, and 34. | Lysine | Ptr2p | Saccharomyces cerevisiae S288C |
| 5 | Simultaneous substitution of arginine for the three lysines fully prevented Ptr2 degradation. | Arginine | Ptr2p | Saccharomyces cerevisiae S288C |
| 6 | Simultaneous substitution of arginine for the three lysines fully prevented Ptr2 degradation. | Lysine | Ptr2p | Saccharomyces cerevisiae S288C |
| 7 | Ptr2 mutants of the presumed peptide-binding site (E92Q, R93K, K205R, W362L, and E480D) exhibited severe defects in peptide import and were subjected to Rsp5-dependent degradation when cells were moved to Ala-Trp medium, whereas, similar to what occurs in the wild-type Ptr2, mutant proteins of the intracellular gate were upregulated. | L-Alanyl-L-tryptophan | Ptr2p | Saccharomyces cerevisiae S288C |