Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY.
| dc.contributor.author | Kumar, Shivesh | |
| dc.contributor.author | Wang, Yan | |
| dc.contributor.author | Zhou, Ye | |
| dc.contributor.author | Dillard, Lucas | |
| dc.contributor.author | Li, Fay-Wei | |
| dc.contributor.author | Sciandra, Carly A | |
| dc.contributor.author | Sui, Ning | |
| dc.contributor.author | Zentella, Rodolfo | |
| dc.contributor.author | Zahn, Emily | |
| dc.contributor.author | Shabanowitz, Jeffrey | |
| dc.contributor.author | Hunt, Donald F | |
| dc.contributor.author | Borgnia, Mario J | |
| dc.contributor.author | Bartesaghi, Alberto | |
| dc.contributor.author | Sun, Tai-Ping | |
| dc.contributor.author | Zhou, Pei | |
| dc.date.accessioned | 2023-04-01T14:18:56Z | |
| dc.date.available | 2023-04-01T14:18:56Z | |
| dc.date.issued | 2023-03 | |
| dc.date.updated | 2023-04-01T14:18:53Z | |
| dc.description.abstract | SPINDLY (SPY) in Arabidopsis thaliana is a novel nucleocytoplasmic protein O-fucosyltransferase (POFUT), which regulates diverse developmental processes. Sequence analysis indicates that SPY is distinct from ER-localized POFUTs and contains N-terminal tetratricopeptide repeats (TPRs) and a C-terminal catalytic domain resembling the O-linked-N-acetylglucosamine (GlcNAc) transferases (OGTs). However, the structural feature that determines the distinct enzymatic selectivity of SPY remains unknown. Here we report the cryo-electron microscopy (cryo-EM) structure of SPY and its complex with GDP-fucose, revealing distinct active-site features enabling GDP-fucose instead of UDP-GlcNAc binding. SPY forms an antiparallel dimer instead of the X-shaped dimer in human OGT, and its catalytic domain interconverts among multiple conformations. Analysis of mass spectrometry, co-IP, fucosylation activity, and cryo-EM data further demonstrates that the N-terminal disordered peptide in SPY contains trans auto-fucosylation sites and inhibits the POFUT activity, whereas TPRs 1-5 dynamically regulate SPY activity by interfering with protein substrate binding. | |
| dc.identifier | 10.1038/s41467-023-37279-1 | |
| dc.identifier.issn | 2041-1723 | |
| dc.identifier.issn | 2041-1723 | |
| dc.identifier.uri | ||
| dc.language | eng | |
| dc.publisher | Springer Science and Business Media LLC | |
| dc.relation.ispartof | Nature communications | |
| dc.relation.isversionof | 10.1038/s41467-023-37279-1 | |
| dc.subject | Humans | |
| dc.subject | Arabidopsis | |
| dc.subject | N-Acetylglucosaminyltransferases | |
| dc.subject | Fucosyltransferases | |
| dc.subject | Fucose | |
| dc.subject | Arabidopsis Proteins | |
| dc.subject | Repressor Proteins | |
| dc.subject | Cryoelectron Microscopy | |
| dc.title | Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY. | |
| dc.type | Journal article | |
| duke.contributor.orcid | Bartesaghi, Alberto|0000-0002-7360-1523 | |
| duke.contributor.orcid | Sun, Tai-Ping|0000-0001-5223-2936 | |
| duke.contributor.orcid | Zhou, Pei|0000-0002-7823-3416 | |
| pubs.begin-page | 1538 | |
| pubs.issue | 1 | |
| pubs.organisational-group | Duke | |
| pubs.organisational-group | School of Medicine | |
| pubs.organisational-group | Trinity College of Arts & Sciences | |
| pubs.organisational-group | Basic Science Departments | |
| pubs.organisational-group | Institutes and Centers | |
| pubs.organisational-group | Biochemistry | |
| pubs.organisational-group | Duke Cancer Institute | |
| pubs.organisational-group | Biology | |
| pubs.organisational-group | Chemistry | |
| pubs.organisational-group | Computer Science | |
| pubs.organisational-group | Institutes and Provost's Academic Units | |
| pubs.organisational-group | University Institutes and Centers | |
| pubs.organisational-group | Duke Institute for Brain Sciences | |
| pubs.publication-status | Published | |
| pubs.volume | 14 |
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