Faculty Opinions recommendation of The MYB36 transcription factor orchestrates Casparian strip formation.

2015 ◽  
Author(s):  
Gwyneth Ingram
Keyword(s):  
Transcription Factor ◽  
Casparian Strip ◽  
Strip Formation

scholarly journals The MYB36 transcription factor orchestrates Casparian strip formation

2015 ◽  
Vol 112 (33) ◽  
pp. 10533-10538 ◽  
Author(s):  
Takehiro Kamiya ◽  
Monica Borghi ◽  
Peng Wang ◽  
John M. C. Danku ◽  
Lothar Kalmbach ◽  
...  
Keyword(s):  
Cell Wall ◽  
Transcription Factor ◽  
Ectopic Expression ◽  
Casparian Strip ◽  
Strip Domain ◽  
Genes Encoding ◽  
Casparian Strips ◽  
Endodermal Cells ◽  
Respiratory Burst Oxidase ◽  
Strip Formation

The endodermis in roots acts as a selectivity filter for nutrient and water transport essential for growth and development. This selectivity is enabled by the formation of lignin-based Casparian strips. Casparian strip formation is initiated by the localization of the Casparian strip domain proteins (CASPs) in the plasma membrane, at the site where the Casparian strip will form. Localized CASPs recruit Peroxidase 64 (PER64), a Respiratory Burst Oxidase Homolog F, and Enhanced Suberin 1 (ESB1), a dirigent-like protein, to assemble the lignin polymerization machinery. However, the factors that control both expression of the genes encoding this biosynthetic machinery and its localization to the Casparian strip formation site remain unknown. Here, we identify the transcription factor, MYB36, essential for Casparian strip formation. MYB36 directly and positively regulates the expression of the Casparian strip genes CASP1, PER64, and ESB1. Casparian strips are absent in plants lacking a functional MYB36 and are replaced by ectopic lignin-like material in the corners of endodermal cells. The barrier function of Casparian strips in these plants is also disrupted. Significantly, ectopic expression of MYB36 in the cortex is sufficient to reprogram these cells to start expressing CASP1–GFP, correctly localize the CASP1–GFP protein to form a Casparian strip domain, and deposit a Casparian strip-like structure in the cell wall at this location. These results demonstrate that MYB36 is controlling expression of the machinery required to locally polymerize lignin in a fine band in the cell wall for the formation of the Casparian strip.

A novel protein family mediates Casparian strip formation in the endodermis

Nature ◽  
2011 ◽  
Vol 473 (7347) ◽  
pp. 380-383 ◽  
Author(s):  
Daniele Roppolo ◽  
Bert De Rybel ◽  
Valérie Dénervaud Tendon ◽  
Alexandre Pfister ◽  
Julien Alassimone ◽  
...  
Keyword(s):  
Protein Family ◽  
Casparian Strip ◽  
Strip Formation ◽  
Novel Protein

scholarly journals OsCASP1 is required for Casparian strip formation at endodermal cells of rice roots for selective uptake of mineral elements

2019 ◽  
pp. tpc.00296.2019 ◽  
Author(s):  
Zhigang Wang ◽  
Naoki Yamaji ◽  
Sheng Huang ◽  
Xiang Zhang ◽  
Mingxing Shi ◽  
...  
Keyword(s):  
Mineral Elements ◽  
Selective Uptake ◽  
Rice Roots ◽  
Casparian Strip ◽  
Endodermal Cells ◽  
Strip Formation

scholarly journals Laccase3-based extracellular domain provides possible positional information for directing Casparian strip formation inArabidopsis

2020 ◽  
Vol 117 (27) ◽  
pp. 15400-15402 ◽  
Author(s):  
Yan Zhuang ◽  
Daqing Zuo ◽  
Yihan Tao ◽  
Huaqing Cai ◽  
Lei Li
Keyword(s):  
Cell Wall ◽  
Tight Junction ◽  
Positional Information ◽  
Extracellular Domain ◽  
Multicopper Oxidase ◽  
Plant Roots ◽  
Membrane Domain ◽  
Casparian Strip ◽  
Endodermal Cells ◽  
Strip Formation

The Casparian strip (CS) is a tight junction-like structure formed by lignin impregnation on the walls of endodermal cells in plant roots. The CS membrane domain (CSDM), demarked by the CASP proteins, is important for orienting lignification enzymes. Here, we report that an endodermis-expressed multicopper oxidase, LACCASE3 (LAC3) inArabidopsis, locates to the interface between lignin domains and the cell wall during early CS development prior to CASP1 localizing to CSDMand eventually flanks the mature CS. Pharmacological perturbation of LAC3 causes dispersed localization of CASP1 and compensatory ectopic lignification. These results support the existence of a LAC3-based CS wall domain which coordinates with CSDMto provide bidirectional positional information that guides precise CS lignification.

Transcription factor/DNA interactions visualized by electron spectroscopic imaging

1992 ◽  
Vol 50 (1) ◽  
pp. 450-451
Author(s):  
David P. Bazett-Jones ◽  
Mark L. Brown
Keyword(s):  
Transcription Factor ◽  
Dna Sequences ◽  
Transcription Initiation ◽  
Molecular Mechanisms ◽  
Phosphorus Content ◽  
Spectroscopic Imaging ◽  
Electron Spectroscopic Imaging ◽  
Dna Backbone ◽  
Two Parameters ◽  
High Level

A multisubunit RNA polymerase enzyme is ultimately responsible for transcription initiation and elongation of RNA, but recognition of the proper start site by the enzyme is regulated by general, temporal and gene-specific trans-factors interacting at promoter and enhancer DNA sequences. To understand the molecular mechanisms which precisely regulate the transcription initiation event, it is crucial to elucidate the structure of the transcription factor/DNA complexes involved. Electron spectroscopic imaging (ESI) provides the opportunity to visualize individual DNA molecules. Enhancement of DNA contrast with ESI is accomplished by imaging with electrons that have interacted with inner shell electrons of phosphorus in the DNA backbone. Phosphorus detection at this intermediately high level of resolution (≈lnm) permits selective imaging of the DNA, to determine whether the protein factors compact, bend or wrap the DNA. Simultaneously, mass analysis and phosphorus content can be measured quantitatively, using adjacent DNA or tobacco mosaic virus (TMV) as mass and phosphorus standards. These two parameters provide stoichiometric information relating the ratios of protein:DNA content.

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