Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain
SGT1 (the suppressor of the G2 allele of Skp1) functions as an adaptor protein that positively regulates plant defense and developmental processes. It comprises three functional domains: the tetratricopeptide repeat (TPR) domain, Chord SGT1 motif (CS), and SGT1-specific motif (SGS). In this study, w...
Saved in:
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-06-01
|
| Series: | Crystals |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4352/15/6/543 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1839654359576608768 |
|---|---|
| author | Yongqi Chang Lifeng Ji Yiling Qin Yaqi Yi Chen Qian Jie Jiang Tian Liu Junfeng Liu Xin Zhang |
| author_facet | Yongqi Chang Lifeng Ji Yiling Qin Yaqi Yi Chen Qian Jie Jiang Tian Liu Junfeng Liu Xin Zhang |
| author_sort | Yongqi Chang |
| collection | DOAJ |
| description | SGT1 (the suppressor of the G2 allele of Skp1) functions as an adaptor protein that positively regulates plant defense and developmental processes. It comprises three functional domains: the tetratricopeptide repeat (TPR) domain, Chord SGT1 motif (CS), and SGT1-specific motif (SGS). In this study, we resolved the crystal structure of the <i>Oryza sativa</i> OsSGT1-TPR domain at 1.53 Å resolution. Structural analysis showed that the TPR domain adopts a homo-dimeric architecture stabilized by salt bridges (mediated by K52/R79/R109) and hydrophobic interactions (involving F17). Functional validation through gel filtration chromatography revealed that the disruption of the dimerization interface via F17A/K52A/R79A mutations caused complete dissociation into monomers, establishing the essential role of TPR-mediated oligomerization in maintaining the structural stability of full-length OsSGT1. Yeast two-hybrid assays showed that the dimerization disruption of SGT1 mutants retained the interaction with OsHSP81-2 (an HSP90 ortholog) and OsRAR1, indicating that SGT1 oligomerization serves primarily as a structural stabilizer rather than a prerequisite for partner interaction. Evolutionary analysis through the sequence alignment of plant SGT1 proteins revealed the conservation of the dimerization interface residues. This study provides structural insights into the conserved molecular features of SGT1 proteins and highlights the functional significance of their oligomerization state. |
| format | Article |
| id | doaj-art-9fb12d7e97914c34bfbd7c2081adceb6 |
| institution | Matheson Library |
| issn | 2073-4352 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Crystals |
| spelling | doaj-art-9fb12d7e97914c34bfbd7c2081adceb62025-06-25T13:41:12ZengMDPI AGCrystals2073-43522025-06-0115654310.3390/cryst15060543Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR DomainYongqi Chang0Lifeng Ji1Yiling Qin2Yaqi Yi3Chen Qian4Jie Jiang5Tian Liu6Junfeng Liu7Xin Zhang8State Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaState Key Laboratory of Maize Bio-Breeding, China Agricultural University, Beijing 100083, ChinaSGT1 (the suppressor of the G2 allele of Skp1) functions as an adaptor protein that positively regulates plant defense and developmental processes. It comprises three functional domains: the tetratricopeptide repeat (TPR) domain, Chord SGT1 motif (CS), and SGT1-specific motif (SGS). In this study, we resolved the crystal structure of the <i>Oryza sativa</i> OsSGT1-TPR domain at 1.53 Å resolution. Structural analysis showed that the TPR domain adopts a homo-dimeric architecture stabilized by salt bridges (mediated by K52/R79/R109) and hydrophobic interactions (involving F17). Functional validation through gel filtration chromatography revealed that the disruption of the dimerization interface via F17A/K52A/R79A mutations caused complete dissociation into monomers, establishing the essential role of TPR-mediated oligomerization in maintaining the structural stability of full-length OsSGT1. Yeast two-hybrid assays showed that the dimerization disruption of SGT1 mutants retained the interaction with OsHSP81-2 (an HSP90 ortholog) and OsRAR1, indicating that SGT1 oligomerization serves primarily as a structural stabilizer rather than a prerequisite for partner interaction. Evolutionary analysis through the sequence alignment of plant SGT1 proteins revealed the conservation of the dimerization interface residues. This study provides structural insights into the conserved molecular features of SGT1 proteins and highlights the functional significance of their oligomerization state.https://www.mdpi.com/2073-4352/15/6/543SGT1TPR domaincrystal structure<i>Oryza sativa</i> |
| spellingShingle | Yongqi Chang Lifeng Ji Yiling Qin Yaqi Yi Chen Qian Jie Jiang Tian Liu Junfeng Liu Xin Zhang Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain Crystals SGT1 TPR domain crystal structure <i>Oryza sativa</i> |
| title | Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain |
| title_full | Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain |
| title_fullStr | Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain |
| title_full_unstemmed | Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain |
| title_short | Crystal Structural Analysis of <i>Oryza sativa</i> SGT1-TPR Domain |
| title_sort | crystal structural analysis of i oryza sativa i sgt1 tpr domain |
| topic | SGT1 TPR domain crystal structure <i>Oryza sativa</i> |
| url | https://www.mdpi.com/2073-4352/15/6/543 |
| work_keys_str_mv | AT yongqichang crystalstructuralanalysisofioryzasativaisgt1tprdomain AT lifengji crystalstructuralanalysisofioryzasativaisgt1tprdomain AT yilingqin crystalstructuralanalysisofioryzasativaisgt1tprdomain AT yaqiyi crystalstructuralanalysisofioryzasativaisgt1tprdomain AT chenqian crystalstructuralanalysisofioryzasativaisgt1tprdomain AT jiejiang crystalstructuralanalysisofioryzasativaisgt1tprdomain AT tianliu crystalstructuralanalysisofioryzasativaisgt1tprdomain AT junfengliu crystalstructuralanalysisofioryzasativaisgt1tprdomain AT xinzhang crystalstructuralanalysisofioryzasativaisgt1tprdomain |