ArticleThe Plant cell2014
The Enzyme-Like Domain of Arabidopsis Nuclear β-Amylases Is Critical for DNA Sequence Recognition and Transcriptional Activation.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 59 citations in OpenAlex.
- SlCV affects starch metabolism by regulating SlBAM3 stability under low night temperature stress in tomatoes.Horticulture research · 2025Article
- Modulation of the Arabidopsis Starch Metabolic Network by the Cytosolic Acetyl-CoA Pathway in the Context of the Diurnal Illumination Cycle.International journal of molecular sciences · 2024Article
- Maize β-amylase7 encodes 2 proteins using alternative transcriptional start sites: Nuclear BAM7 and plastidic BAM2.Plant physiology · 2023Article
- Genome-wide identification and expression analysis of BZR gene family and associated responses to abiotic stresses in cucumber (Cucumis sativus L.).BMC plant biology · 2023Article
- Genome-wide characterization and expression analysis of α-amylase and β-amylase genes underlying drought tolerance in cassava.BMC genomics · 2023Article
- Diversification in the inositol tris/tetrakisphosphate kinase (ITPK) family: crystal structure and enzymology of the outlier AtITPK4.The Biochemical journal · 2023Article
- BES1/BZR1 Family Transcription Factors Regulate Plant Development via Brassinosteroid-Dependent and Independent Pathways.International journal of molecular sciences · 2022Review
- The BAM7 gene in Zea mays encodes a protein with similar structural and catalytic properties to Arabidopsis BAM2.Acta crystallographica. Section D, Structural biology · 2022Article
- BETA-AMYLASE9 is a plastidial nonenzymatic regulator of leaf starch degradation.Plant physiology · 2022Article
- Article
- Genome-Wide Identification and Characterization of the Brassinazole-resistant (International journal of molecular sciences · 2021Article
- Promoter Architecture and Transcriptional Regulation of Genes Upregulated in Germination and Coleoptile Elongation of Diverse Rice Genotypes Tolerant to Submergence.Frontiers in genetics · 2021Article
- Maize ZmBES1/BZR1-5 Decreases ABA Sensitivity and Confers Tolerance to Osmotic Stress in TransgenicInternational journal of molecular sciences · 2020Article
- Involvement of five catalytically active Arabidopsis β-amylases in leaf starch metabolism and plant growth.Plant direct · 2020Article
- Emerging strategies for the identification of protein-metabolite interactions.Journal of experimental botany · 2019Article
- LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation.The Plant cell · 2019Article
- Article
- The evolution of functional complexity within the β-amylase gene family in land plants.BMC evolutionary biology · 2019Article
- Phylogenetic Analyses and GAGA-Motif Binding Studies of BBR/BPC Proteins Lend to Clues in GAGA-Motif Recognition and a Regulatory Role in Brassinosteroid Signaling.Frontiers in plant science · 2019Article
- Characterization ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2018Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant BZR1-BAM transcription factors contain a β-amylase (BAM)-like domain, characteristic of proteins involved in starch breakdown. The enzyme-derived domains appear to be noncatalytic, but they determine the function of the two Arabidopsis thaliana BZR1-BAM isoforms (BAM7 and BAM8) during transcriptional initiation. Removal or swapping of the BAM domains demonstrates that the BAM7 BAM domain restricts DNA binding and transcriptional activation, while the BAM8 BAM domain allows both activities. Furthermore, we demonstrate that BAM7 and BAM8 interact on the protein level and cooperate during transcriptional regulation. Site-directed mutagenesis of residues in the BAM domain of BAM8 shows that its function as a transcriptional activator is independent of catalysis but requires an intact substrate binding site, suggesting it may bind a ligand. Microarray experiments with plants overexpressing truncated versions lacking the BAM domain indicate that the pseudo-enzymatic domain increases selectivity for the preferred cis-regulatory element BBRE (BZR1-BAM Responsive Element). Side specificity toward the G-box may allow crosstalk to other signaling networks. This work highlights the importance of the enzyme-derived domain of BZR1-BAMs, supporting their potential role as metabolic sensors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.