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| Item Type: | Article |
|---|---|
| Title: | Characterization of the self-palmitoylation activity of the transport protein particle component Bet3 |
| Creators Name: | Kuemmel, D. and Walter, J. and Heck, M. and Heinemann, U. and Veit, M. |
| Abstract: | Bet3, a transport protein particle component involved in vesicular trafficking, contains a hydrophobic tunnel occupied by a fatty acid linked to cysteine 68. We reported that Bet3 has a unique self-palmitoylating activity. Here we show that mutation of arginine 67 reduced self-palmitoylation of Bet3, but the effect was compensated by increasing the pH. Thus, arginine helps to deprotonate cysteine such that it could function as a nucleophile in the acylation reaction which is supported by the structural analysis of non-acylated Bet3. Using fluorescence spectroscopy we show that long-chain acyl-CoAs bind with micromolar affinity to Bet3, whereas shorter-chain acyl-CoAs do not interact. Mutants with a deleted acylation site or a blocked tunnel bind to Pal-CoA, only the latter with slightly reduced affinity. Bet3 contains three binding sites for Pal-CoA, but their number was reduced to two in the mutant with an obstructed tunnel, indicating that Bet3 contains binding sites on its surface. |
| Keywords: | Golgi, Vesicular Transport, Tethering, TRAPP, Bet3, Palmitoylation, Acyl-CoA |
| Source: | Cellular and Molecular Life Sciences |
| ISSN: | 1420-682X |
| Publisher: | Birkhäuser |
| Volume: | 67 |
| Number: | 15 |
| Page Range: | 2653-2664 |
| Date: | August 2010 |
| Official Publication: | https://doi.org/10.1007/s00018-010-0358-y |
| PubMed: | View item in PubMed |
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