Biochemical characterization of recombinant polypeptides correspondingto the predicted ²±± fold in Aux/IAA proteins

Morgan, Kristin E.; Zarembinski, Thomas I.; Theologis, Athanasios; Abel, Steffen

doi:10.1016/s0014-5793(99)00819-4

Cited by 28 publications

(5 citation statements)

References 27 publications

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“…Domain Ⅱ, essential in auxin signaling transduction, contained 13 specific amino acid core sequences ‘VGWPP’ that constitute a degradation unit targeted by the ubiquitin-ligase SCF TIR1 ( Ouellet et al, 2001 ; Dharmasiri et al, 2003 ). Domain III can dimerize in vitro and have a turning-helix-helix (βαα) region ( Morgan et al, 1999 ). Domain Ⅲ and Domain Ⅳ are homologous to the C-terminal domain of ARFs, which enables Aux/IAA to dimerize or polymerize and bind ARFs to inhibit their functions ( Woodward and Bartel, 2005 ).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification of Aux/IAA gene family and their expression analysis in Prunus mume

et al. 2022

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AUXIN/INDOLE ACETIC ACIDs (Aux/IAAs), an early auxin-responsive gene family, is important for plant growth and development. To fully comprehend the character of Aux/IAA genes in woody plants, we identified 19 PmIAA genes in Prunus mume and dissected their protein domains, phylogenetic relationship, gene structure, promoter, and expression patterns during floral bud flushing, auxin response, and abiotic stress response. The study showed that PmIAA proteins shared conserved Aux/IAA domain, but differed in protein motif composition. 19 PmIAA genes were divided into six groups (Groups Ⅰ to Ⅵ) based on phylogenetic analysis. The gene duplication analysis showed that segmental and dispersed duplication greatly influenced the expansion of PmIAA genes. Moreover, we identified and classified the cis-elements of PmIAA gene promoters and detected elements that are related to phytohormone responses and abiotic stress responses. With expression pattern analysis, we observed the auxin-responsive expression of PmIAA5, PmIAA17, and PmIAA18 in flower bud, stem, and leaf tissues. PmIAA5, PmIAA13, PmIAA14, and PmIAA18 were possibly involved in abiotic stress responses in P. mume. In general, these results laid the theoretical foundation for elaborating the functions of Aux/IAA genes in perennial woody plant development.

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Section: Introductionmentioning

confidence: 99%

Genome-wide identification of Aux/IAA gene family and their expression analysis in Prunus mume

et al. 2022

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“…We determined the solution structure of the 13 C, 15 N isotope-labeled C-terminal domain pair of PsIAA4, which comprises amino acid residues 86–189 (DIII/IV), by using an acidic buffer system to prevent aggregation of the affinity-purified, (His) 6 -tagged wild-type protein. Aggregation was reported over a broad pH range for other AUX/IAA proteins and truncated derivatives in vitro ( 6 , 31 ). Compared to neutral pH conditions, sedimentation equilibrium analysis confirmed the monomeric and homogeneous state of PsIAA4 DIII/IV at low pH ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response

Dinesh

Kovermann²,

Gopalswamy³

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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SignificanceIndole-3-acetic acid (IAA or auxin) is indispensable during the entire plant life cycle and regulates diverse processes and transitions via hierarchical gene expression. The hormone triggers rapid destruction of AUXIN/INDOLE-3-ACETIC ACID (AUX/IAA) repressors that control AUXIN RESPONSE FACTOR (ARF) activators in auxin-regulated gene transcription. AUX/IAA and ARF proteins interact physically via their C-terminal Phox and Bem1p (PB1) domain, which is shared between both families. This work reports the solution structure of a wild-type AUX/IAA PB1 domain and identifies amino acid residues that engage in directional interaction of monomers, largely via hydrogen bonds between conserved basic and acidic surface patches. Our study provides a framework for unraveling molecular determinants that confer specificity to complex interactions between AUX/IAA and ARF transcription factors.

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“…More recently, flexible hotspots with certain specific lysine residues have been identified in the degron-flanking regions, which are closely linked to ubiquitylation mediated by TIR1 [ 56 ]. Domain III contains an amphipathic βαα-fold with a structure and function similar to the DNA recognition motif in Arc and MetJ repressors [ 7 , 57 ]. Further studies confirmed the roles of the βαα-fold in homo- and heterodimerization with Aux/IAA and/or ARF proteins [ 51 , 57 , 58 ].…”

Section: Identification Gene Duplication and Molecular Structurementioning

confidence: 99%

“…Domain III contains an amphipathic βαα-fold with a structure and function similar to the DNA recognition motif in Arc and MetJ repressors [ 7 , 57 ]. Further studies confirmed the roles of the βαα-fold in homo- and heterodimerization with Aux/IAA and/or ARF proteins [ 51 , 57 , 58 ]. Domain IV comprises an acidic region and an SV40 type NLS (PKKKRKV) [ 59 ].…”

Section: Identification Gene Duplication and Molecular Structurementioning

confidence: 99%

Aux/IAA Gene Family in Plants: Molecular Structure, Regulation, and Function

Luo

Zhou

Zhang

2018

IJMS

373

249

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Auxin plays a crucial role in the diverse cellular and developmental responses of plants across their lifespan. Plants can quickly sense and respond to changes in auxin levels, and these responses involve several major classes of auxin-responsive genes, including the Auxin/Indole-3-Acetic Acid (Aux/IAA) family, the auxin response factor (ARF) family, small auxin upregulated RNA (SAUR), and the auxin-responsive Gretchen Hagen3 (GH3) family. Aux/IAA proteins are short-lived nuclear proteins comprising several highly conserved domains that are encoded by the auxin early response gene family. These proteins have specific domains that interact with ARFs and inhibit the transcription of genes activated by ARFs. Molecular studies have revealed that Aux/IAA family members can form diverse dimers with ARFs to regulate genes in various ways. Functional analyses of Aux/IAA family members have indicated that they have various roles in plant development, such as root development, shoot growth, and fruit ripening. In this review, recently discovered details regarding the molecular characteristics, regulation, and protein–protein interactions of the Aux/IAA proteins are discussed. These details provide new insights into the molecular basis of the Aux/IAA protein functions in plant developmental processes.

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Biochemical characterization of recombinant polypeptides correspondingto the predicted ²±± fold in Aux/IAA proteins

Cited by 28 publications

References 27 publications

Genome-wide identification of Aux/IAA gene family and their expression analysis in Prunus mume

Genome-wide identification of Aux/IAA gene family and their expression analysis in Prunus mume

Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response

Aux/IAA Gene Family in Plants: Molecular Structure, Regulation, and Function

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