Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions.
The Auxin/Indole-3-Acetic Acid (Aux/IAA) and Auxin Response Factor (ARF) are two important families that play key roles in auxin signal transduction. Both of the families contain a similar carboxyl-terminal domain (Domain III/IV) that facilitates interactions between these two families. In spite of...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3893212?pdf=render |
| _version_ | 1819112075542134784 |
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| author | Jun Ni Zhenxing Zhu Gaohang Wang Yanxia Shen Yanyan Zhang Ping Wu |
| author_facet | Jun Ni Zhenxing Zhu Gaohang Wang Yanxia Shen Yanyan Zhang Ping Wu |
| author_sort | Jun Ni |
| collection | DOAJ |
| description | The Auxin/Indole-3-Acetic Acid (Aux/IAA) and Auxin Response Factor (ARF) are two important families that play key roles in auxin signal transduction. Both of the families contain a similar carboxyl-terminal domain (Domain III/IV) that facilitates interactions between these two families. In spite of the importance of protein-protein interactions among these transcription factors, the mechanisms involved in these interactions are largely unknown. In this study, we isolated six intragenic suppressors of an auxin insensitive mutant, Osiaa23. Among these suppressors, Osiaa23-R5 successfully rescued all the defects of the mutant. Sequence analysis revealed that an amino acid substitution occurred in the Tryptophan (W) residue in Domain IV of Osiaa23. Yeast two-hybrid experiments showed that the mutation in Domain IV prevents the protein-protein interactions between Osiaa23 and OsARFs. Phylogenetic analysis revealed that the W residue is conserved in both OsIAAs and OsARFs. Next, we performed site-specific amino acid substitutions within Domain IV of OsARFs, and the conserved W in Domain IV was exchanged by Serine (S). The mutated OsARF(WS)s can be released from the inhibition of Osiaa23 and maintain the transcriptional activities. Expression of OsARF(WS)s in Osiaa23 mutant rescued different defects of the mutant. Our results suggest a previously unknown importance of Domain IV in both families and provide an indirect way to investigate functions of OsARFs. |
| first_indexed | 2024-12-22T04:07:45Z |
| format | Article |
| id | doaj.art-0639be142f10420ca6b2070f7a4572de |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T04:07:45Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-0639be142f10420ca6b2070f7a4572de2022-12-21T18:39:35ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0191e8535810.1371/journal.pone.0085358Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions.Jun NiZhenxing ZhuGaohang WangYanxia ShenYanyan ZhangPing WuThe Auxin/Indole-3-Acetic Acid (Aux/IAA) and Auxin Response Factor (ARF) are two important families that play key roles in auxin signal transduction. Both of the families contain a similar carboxyl-terminal domain (Domain III/IV) that facilitates interactions between these two families. In spite of the importance of protein-protein interactions among these transcription factors, the mechanisms involved in these interactions are largely unknown. In this study, we isolated six intragenic suppressors of an auxin insensitive mutant, Osiaa23. Among these suppressors, Osiaa23-R5 successfully rescued all the defects of the mutant. Sequence analysis revealed that an amino acid substitution occurred in the Tryptophan (W) residue in Domain IV of Osiaa23. Yeast two-hybrid experiments showed that the mutation in Domain IV prevents the protein-protein interactions between Osiaa23 and OsARFs. Phylogenetic analysis revealed that the W residue is conserved in both OsIAAs and OsARFs. Next, we performed site-specific amino acid substitutions within Domain IV of OsARFs, and the conserved W in Domain IV was exchanged by Serine (S). The mutated OsARF(WS)s can be released from the inhibition of Osiaa23 and maintain the transcriptional activities. Expression of OsARF(WS)s in Osiaa23 mutant rescued different defects of the mutant. Our results suggest a previously unknown importance of Domain IV in both families and provide an indirect way to investigate functions of OsARFs.http://europepmc.org/articles/PMC3893212?pdf=render |
| spellingShingle | Jun Ni Zhenxing Zhu Gaohang Wang Yanxia Shen Yanyan Zhang Ping Wu Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. PLoS ONE |
| title | Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. |
| title_full | Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. |
| title_fullStr | Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. |
| title_full_unstemmed | Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. |
| title_short | Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions. |
| title_sort | intragenic suppressor of osiaa23 revealed a conserved tryptophan residue crucial for protein protein interactions |
| url | http://europepmc.org/articles/PMC3893212?pdf=render |
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