dc.contributor.author |
Lee, Hui Wen |
|
dc.contributor.author |
Sharma, Prachi |
|
dc.contributor.author |
Janssen, Bart J |
|
dc.contributor.author |
Drummond, Revel SM |
|
dc.contributor.author |
Luo, Zhiwei |
|
dc.contributor.author |
Hamiaux, Cyril |
|
dc.contributor.author |
Collier, Thomas |
|
dc.contributor.author |
Allison, Jane R |
|
dc.contributor.author |
Newcomb, Richard D |
|
dc.contributor.author |
Snowden, Kimberley C |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-05-19T22:04:07Z |
|
dc.date.available |
2022-05-19T22:04:07Z |
|
dc.date.issued |
2020-03 |
|
dc.identifier.citation |
(2020). Journal of Biological Chemistry, 295(13), 4181-4193. |
|
dc.identifier.issn |
0021-9258 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59369 |
|
dc.description.abstract |
Strigolactones (SLs) are terpenoid-derived plant hormones that regulate various developmental processes, particularly shoot branching, root development, and leaf senescence. The SL receptor has an unusual mode of action. Upon binding SL, it hydrolyzes the hormone, and then covalently binds one of the hydrolytic products. These initial events enable the SL receptor DAD2 (in petunia) to interact with the F-box protein PhMAX2A of the Skp-Cullin-F-box (SCF) complex and/or a repressor of SL signaling, PhD53A. However, it remains unclear how binding and hydrolysis structurally alters the SL receptor to enable its engagement with signaling partners. Here, we used mutagenesis to alter DAD2 and affect SL hydrolysis or DAD2's ability to interact with its signaling partners. We identified three DAD2 variants whose hydrolytic activity had been separated from the receptor's interactions with PhMAX2A or PhD53A. Two variants, DAD2<sup>N242I</sup> and DAD2<sup>F135A</sup>, having substitutions in the core α/β hydrolase-fold domain and the hairpin, exhibited hormone-independent interactions with PhMAX2A and PhD53A, respectively. Conversely, the DAD2<sup>D166A</sup> variant could not interact with PhMAX2A in the presence of SL, but its interaction with PhD53A remained unaffected. Structural analyses of DAD2<sup>N242I</sup> and DAD2<sup>D166A</sup> revealed only small differences compared with the structure of the WT receptor. Results of molecular dynamics simulations of the DAD2<sup>N242I</sup> structure suggested that increased flexibility is a likely cause for its SL-independent interaction with PhMAX2A. Our results suggest that PhMAX2A and PhD53A have distinct binding sites on the SL receptor and that its flexibility is a major determinant of its interactions with these two downstream regulators. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
Elsevier BV |
|
dc.relation.ispartofseries |
The Journal of biological chemistry |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
|
dc.subject |
Petunia |
|
dc.subject |
Lactones |
|
dc.subject |
Heterocyclic Compounds, 3-Ring |
|
dc.subject |
Hydrolases |
|
dc.subject |
SKP Cullin F-Box Protein Ligases |
|
dc.subject |
Plant Growth Regulators |
|
dc.subject |
F-Box Proteins |
|
dc.subject |
Plant Proteins |
|
dc.subject |
Signal Transduction |
|
dc.subject |
Gene Expression Regulation, Plant |
|
dc.subject |
Protein Binding |
|
dc.subject |
DAD2 |
|
dc.subject |
Petunia hybrida |
|
dc.subject |
crystallography |
|
dc.subject |
molecular dynamics |
|
dc.subject |
mutagenesis |
|
dc.subject |
phytohormone signaling |
|
dc.subject |
plant hormone |
|
dc.subject |
receptor |
|
dc.subject |
strigolactone |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
HORMONE-RECEPTOR |
|
dc.subject |
LEAF SENESCENCE |
|
dc.subject |
INHIBITION |
|
dc.subject |
DWARF14 |
|
dc.subject |
RICE |
|
dc.subject |
ARABIDOPSIS |
|
dc.subject |
DEGRADATION |
|
dc.subject |
GERMINATION |
|
dc.subject |
REPRESSOR |
|
dc.subject |
SYSTEM |
|
dc.subject |
0601 Biochemistry and Cell Biology |
|
dc.subject |
0607 Plant Biology |
|
dc.subject |
Biomedical |
|
dc.subject |
Basic Science |
|
dc.subject |
03 Chemical Sciences |
|
dc.subject |
06 Biological Sciences |
|
dc.subject |
11 Medical and Health Sciences |
|
dc.title |
Flexibility of the petunia strigolactone receptor DAD2 promotes its interaction with signaling partners. |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1074/jbc.ra119.011509 |
|
pubs.issue |
13 |
|
pubs.begin-page |
4181 |
|
pubs.volume |
295 |
|
dc.date.updated |
2022-04-27T23:07:26Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
32071083 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/32071083 |
|
pubs.end-page |
4193 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Research Support, Non-U.S. Gov't |
|
pubs.subtype |
research-article |
|
pubs.subtype |
Journal Article |
|
pubs.elements-id |
797629 |
|
pubs.org-id |
Medical and Health Sciences |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
pubs.org-id |
Medical Sciences |
|
pubs.org-id |
Molecular Medicine |
|
dc.identifier.eissn |
1083-351X |
|
dc.identifier.pii |
S0021-9258(17)48746-1 |
|
pubs.record-created-at-source-date |
2022-04-28 |
|