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AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
Archives of Biochemistry and Biophysics, Volume: 443, Issue: 1-2, Pages: 74 - 81
Swansea University Author: Steve Slocombe
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DOI (Published version): 10.1016/j.abb.2005.09.003
Abstract
Long-chain acyl-CoA synthetases (LACSs) activate fatty acids for further metabolism and are encoded by a multi-gene family in Arabidopsis. AtLACS6 possesses a type 2 (PTS2) peroxisomal targeting sequence, whilst AtLACS7 has both a type 1 and type 2 peroxisomal targeting sequence. AtLACS7 was used as...
| Published in: | Archives of Biochemistry and Biophysics |
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| ISSN: | 0003-9861 |
| Published: |
Elsevier BV
2005
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| Online Access: |
Check full text
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| URI: | https://cronfa.swan.ac.uk/Record/cronfa65483 |
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| Abstract: |
Long-chain acyl-CoA synthetases (LACSs) activate fatty acids for further metabolism and are encoded by a multi-gene family in Arabidopsis. AtLACS6 possesses a type 2 (PTS2) peroxisomal targeting sequence, whilst AtLACS7 has both a type 1 and type 2 peroxisomal targeting sequence. AtLACS7 was used as bait in a yeast two-hybrid screen. Multiple clones of the PTS1 receptor PEX5 were isolated. Quantitative beta-galactosidase assay indicated that full-length PEX5 interacts with AtLACS7 with higher affinity than the TPR domains alone. The interaction between PEX5 and AtLACS7 was confirmed by co-immunoprecipitation and shown to be specific for the PTS1, therefore the AtLACS7 PTS1 is accessible to bind PEX5 in the full-length AtLACS7 protein. The expression profile of AtLACS6, AtLACS7, AtPEX5, and AtPEX7 revealed that AtLACS6 and 7 have distinct patterns of expression and we speculate that the possession of two targeting signals may be advantageous for the import of AtLACS7 when receptors may be limiting. |
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| Keywords: |
Acyl-CoA synthetase; Fatty acid metabolism; Glyoxysome; PEX5; PTS1; Peroxisome protein targeting; Arabidopsis |
| College: |
Faculty of Science and Engineering |
| Issue: |
1-2 |
| Start Page: |
74 |
| End Page: |
81 |