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AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5

Stefania Bonsegna, Steve Slocombe, Luigi De Bellis, Alison Baker

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...

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Published in: Archives of Biochemistry and Biophysics
ISSN: 0003-9861
Published: Elsevier BV 2005
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URI: https://cronfa.swan.ac.uk/Record/cronfa65483
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first_indexed 2024-01-22T14:09:43Z
last_indexed 2024-01-22T14:09:43Z
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spelling v2 65483 2024-01-22 AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5 4a1ea486a78ed357efdfa053a277ae40 Steve Slocombe Steve Slocombe true false 2024-01-22 SBI 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. Journal Article Archives of Biochemistry and Biophysics 443 1-2 74 81 Elsevier BV 0003-9861 Acyl-CoA synthetase; Fatty acid metabolism; Glyoxysome; PEX5; PTS1; Peroxisome protein targeting; Arabidopsis 15 11 2005 2005-11-15 10.1016/j.abb.2005.09.003 COLLEGE NANME Biosciences COLLEGE CODE SBI Swansea University 2024-03-21T17:00:56.6018908 2024-01-22T14:08:54.0963526 Faculty of Science and Engineering School of Biosciences, Geography and Physics - Biosciences Stefania Bonsegna 1 Steve Slocombe 2 Luigi De Bellis 3 Alison Baker 4
title AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
spellingShingle AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
Steve Slocombe
title_short AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
title_full AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
title_fullStr AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
title_full_unstemmed AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
title_sort AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5
author_id_str_mv 4a1ea486a78ed357efdfa053a277ae40
author_id_fullname_str_mv 4a1ea486a78ed357efdfa053a277ae40_***_Steve Slocombe
author Steve Slocombe
author2 Stefania Bonsegna
Steve Slocombe
Luigi De Bellis
Alison Baker
format Journal article
container_title Archives of Biochemistry and Biophysics
container_volume 443
container_issue 1-2
container_start_page 74
publishDate 2005
institution Swansea University
issn 0003-9861
doi_str_mv 10.1016/j.abb.2005.09.003
publisher Elsevier BV
college_str Faculty of Science and Engineering
hierarchytype
hierarchy_top_id facultyofscienceandengineering
hierarchy_top_title Faculty of Science and Engineering
hierarchy_parent_id facultyofscienceandengineering
hierarchy_parent_title Faculty of Science and Engineering
department_str School of Biosciences, Geography and Physics - Biosciences{{{_:::_}}}Faculty of Science and Engineering{{{_:::_}}}School of Biosciences, Geography and Physics - Biosciences
document_store_str 0
active_str 0
description 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.
published_date 2005-11-15T17:00:57Z
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score 11.013148

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