scholarly journals A new link between stress response and nucleolar function during pollen development inArabidopsismediated by AtREN1 protein

2013 ◽  
Vol 37 (3) ◽  
pp. 670-683 ◽  
Author(s):  
DAVID REŇÁK ◽  
ANTÓNIA GIBALOVÁ ◽  
KATARZYNA ŠOLCOVÁ ◽  
DAVID HONYS
Keyword(s):  
Stress Response ◽  
Pollen Development ◽  
Nucleolar Function

scholarly journals The Role of Endoplasmic Reticulum Stress Response in Pollen Development and Heat Stress Tolerance

2021 ◽  
Vol 12 ◽  
Author(s):  
Mohan B. Singh ◽  
Neeta Lohani ◽  
Prem L. Bhalla
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Heat Stress ◽  
Stress Response ◽  
Er Stress ◽  
Pollen Development ◽  
Gene Knockout ◽  
Stress Conditions ◽  
Endoplasmic Reticulum Stress Response

Endoplasmic reticulum (ER) stress is defined by a protracted disruption in protein folding and accumulation of unfolded or misfolded proteins in the ER. This accumulation of unfolded proteins can result from excessive demands on the protein folding machinery triggered by environmental and cellular stresses such as nutrient deficiencies, oxidative stress, pathogens, and heat. The cell responds to ER stress by activating a protective pathway termed unfolded protein response (UPR), which comprises cellular mechanisms targeted to maintain cellular homeostasis by increasing the ER’s protein folding capacity. The UPR is especially significant for plants as being sessile requires them to adapt to multiple environmental stresses. While multiple stresses trigger the UPR at the vegetative stage, it appears to be active constitutively in the anthers of unstressed plants. Transcriptome analysis reveals significant upregulation of ER stress-related transcripts in diploid meiocytes and haploid microspores. Interestingly, several ER stress-related genes are specifically upregulated in the sperm cells. The analysis of gene knockout mutants in Arabidopsis has revealed that defects in ER stress response lead to the failure of normal pollen development and enhanced susceptibility of male gametophyte to heat stress conditions. In this mini-review, we provide an overview of the role of ER stress and UPR in pollen development and its protective roles in maintaining male fertility under heat stress conditions.

scholarly journals Ensuring Reproduction at High Temperatures: The Heat Stress Response during Anther and Pollen Development

Plants ◽  
2013 ◽  
Vol 2 (3) ◽  
pp. 489-506 ◽  
Author(s):  
Filomena Giorno ◽  
Mieke Wolters-Arts ◽  
Celestina Mariani ◽  
Ivo Rieu
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
High Temperatures ◽  
Pollen Development ◽  
Heat Stress Response

scholarly journals Untargeted metabolomic analysis of tomato pollen development and heat stress response

2017 ◽  
Vol 30 (2) ◽  
pp. 81-94 ◽  
Author(s):  
Marine J. Paupière ◽  
Florian Müller ◽  
Hanjing Li ◽  
Ivo Rieu ◽  
Yury M. Tikunov ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Pollen Development ◽  
Metabolomic Analysis ◽  
Heat Stress Response

scholarly journals Heat Stress Response Mechanisms in Pollen Development

2021 ◽  
Author(s):  
Palak Chaturvedi ◽  
Anna J. Wiese ◽  
Arindam Ghatak ◽  
Lenka Záveská Drábková ◽  
Wolfram Weckwerth ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Pollen Development ◽  
Heat Stress Response

Resolution of Channels in the Exine by Translocation of Colloidal Iron

1971 ◽  
Vol 29 ◽  
pp. 352-353
Author(s):  
John R. Rowley
Keyword(s):  
Phosphate Buffer ◽  
Pollen Development ◽  
Osmium Tetroxide ◽  
Pollen Grains ◽  
Deionized Water ◽  
Colloidal Iron ◽  
Fixed Material ◽  
Epilobium Angustifolium ◽  
Untreated Material ◽  
Microspore Mitosis

The morphology of the exine of many pollen grains, at the time of flowering, is such that one can suppose that transport of substances through the exine occurred during pollen development. Holes or channels, microscopic to submicroscopic, are described for a large number of grains. An inner part of the exine of Epilobium angustifolium L. and E. montanum L., which may be referred to as the endexine, has irregularly shaped channels early in pollen development although by microspore mitosis there is no indication of such channeling in chemically fixed material. The nucleus in microspores used in the experiment reported here was in prophase of microspore mitosis and the endexine, while lamellated in untreated grains, did not contain irregularly shaped channels. Untreated material from the same part of the inflorescence as iron treated stamens was examined following fixation with 0.1M glutaraldehyde in cacodylate-HCl buffer at pH 6.9 (315 milliosmoles) for 24 hrs, 4% formaldehyde in phosphate buffer at pH 7.2 (1,300 milliosmoles) for 12 hrs, 1% glutaraldehyde mixed with 0.1% osmium tetroxide for 20 min, osmium tetroxide in deionized water for 2 hrs and 1% glutaraldehyde mixed with 4% formaldehyde in 0.1M cacodylate-HCl buffer at pH 6.9 for two hrs.

CarR, a MarR-family regulator from Corynebacterium glutamicum, modulated antibiotic and aromatic compound resistance

2019 ◽  
Vol 476 (21) ◽  
pp. 3141-3159 ◽  
Author(s):  
Meiru Si ◽  
Can Chen ◽  
Zengfan Wei ◽  
Zhijin Gong ◽  
GuiZhi Li ◽  
...  
Keyword(s):  
Stress Response ◽  
Ligand Binding ◽  
Corynebacterium Glutamicum ◽  
Conformational Changes ◽  
Cysteine Oxidation ◽  
Transcriptional Regulatory ◽  
Ligand Free ◽  
Redox Sensing

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.

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