Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content
Using in vitro protein complex formation assay, ability of SNAP-25 isoforms to generate SDS-resistant ternary SNARE complexes with Syntaxin-1 and VAMP-2 was investigated. Major SNAP-25 family proteins were found to generate heat-resistant ternary complexes with varying efficiency. Compared to human...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-12-01
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| Series: | Biochemistry and Biophysics Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580821002442 |
| _version_ | 1818352691931250688 |
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| author | Vadakkanchery V. Vaidyanathan Thomas Binz |
| author_facet | Vadakkanchery V. Vaidyanathan Thomas Binz |
| author_sort | Vadakkanchery V. Vaidyanathan |
| collection | DOAJ |
| description | Using in vitro protein complex formation assay, ability of SNAP-25 isoforms to generate SDS-resistant ternary SNARE complexes with Syntaxin-1 and VAMP-2 was investigated. Major SNAP-25 family proteins were found to generate heat-resistant ternary complexes with varying efficiency. Compared to human SNAP-25, its non-neuronal counterparts SNAP-23 and SNAP-29 formed lower amounts of ternary complexes. Changing Pro182 in human SNAP-23 to Arg182 (SNAP-23 P182R) improved its ability to bind partners and form complexes. In silico analysis of C-terminal helical content in various SNAP-25 family members showed that except human SNAP-23, all others displayed secondary α-helical conformation. We also report that human SNAP-29 is resistant to the proteolytic action of botulinum neurotoxin A even when applied at large concentration. |
| first_indexed | 2024-12-13T18:57:40Z |
| format | Article |
| id | doaj.art-88e7b85be692443885c80a49cc5b6f5a |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-12-13T18:57:40Z |
| publishDate | 2021-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-88e7b85be692443885c80a49cc5b6f5a2022-12-21T23:34:46ZengElsevierBiochemistry and Biophysics Reports2405-58082021-12-0128101150Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil contentVadakkanchery V. Vaidyanathan0Thomas Binz1Corresponding author. Vipragen Biosciences Pvt. Ltd., #67B, Hootagalli Industrial Area, Mysuru, 570018, India.; Institute of Cellular Biochemistry, Hannover Medical School, Hannover, 30625, GermanyInstitute of Cellular Biochemistry, Hannover Medical School, Hannover, 30625, GermanyUsing in vitro protein complex formation assay, ability of SNAP-25 isoforms to generate SDS-resistant ternary SNARE complexes with Syntaxin-1 and VAMP-2 was investigated. Major SNAP-25 family proteins were found to generate heat-resistant ternary complexes with varying efficiency. Compared to human SNAP-25, its non-neuronal counterparts SNAP-23 and SNAP-29 formed lower amounts of ternary complexes. Changing Pro182 in human SNAP-23 to Arg182 (SNAP-23 P182R) improved its ability to bind partners and form complexes. In silico analysis of C-terminal helical content in various SNAP-25 family members showed that except human SNAP-23, all others displayed secondary α-helical conformation. We also report that human SNAP-29 is resistant to the proteolytic action of botulinum neurotoxin A even when applied at large concentration.http://www.sciencedirect.com/science/article/pii/S2405580821002442SNAP-25 and SNAP-23 proteinsSDS-Resistant ternary SNARE complexesC-terminal coiled-coil contentBotulinum neurotoxin cleavage |
| spellingShingle | Vadakkanchery V. Vaidyanathan Thomas Binz Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content Biochemistry and Biophysics Reports SNAP-25 and SNAP-23 proteins SDS-Resistant ternary SNARE complexes C-terminal coiled-coil content Botulinum neurotoxin cleavage |
| title | Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content |
| title_full | Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content |
| title_fullStr | Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content |
| title_full_unstemmed | Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content |
| title_short | Ability of human SNAP-23 to generate high molecular weight SDS-resistant ternary SNARE complexes is influenced by C-terminal coil content |
| title_sort | ability of human snap 23 to generate high molecular weight sds resistant ternary snare complexes is influenced by c terminal coil content |
| topic | SNAP-25 and SNAP-23 proteins SDS-Resistant ternary SNARE complexes C-terminal coiled-coil content Botulinum neurotoxin cleavage |
| url | http://www.sciencedirect.com/science/article/pii/S2405580821002442 |
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