In-gel NHS-propionate derivatization for histone post-translational modifications analysis in Arabidopsis thaliana

2015 ◽  
Vol 886 ◽  
pp. 107-113 ◽  
Author(s):  
Jiajia Chen ◽  
Jun Gao ◽  
Maolin Peng ◽  
Yi Wang ◽  
Yanyan Yu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Post Translational Modifications

scholarly journals Post-Translational Modifications of the Endogenous and Transgenic FLC Protein in Arabidopsis thaliana

2008 ◽  
Vol 49 (12) ◽  
pp. 1859-1866 ◽  
Author(s):  
Masumi Robertson ◽  
Chris A. Helliwell ◽  
Elizabeth S. Dennis
Keyword(s):  
Arabidopsis Thaliana ◽  
Post Translational Modifications

Phosphoproteomic studies in Arabidopsis and tobacco male gametophytes

2014 ◽  
Vol 42 (2) ◽  
pp. 383-387 ◽  
Author(s):  
Jan Fíla ◽  
Věra Čapková ◽  
David Honys
Keyword(s):  
Amino Acids ◽  
Arabidopsis Thaliana ◽  
Cell Wall ◽  
Nicotiana Tabacum ◽  
Pollen Tube ◽  
Protein Phosphorylation ◽  
Pollen Tube Growth ◽  
Mature Pollen ◽  
Phosphorylation Sites ◽  
Post Translational Modifications

Mature pollen represents an extremely resistant quiescent structure surrounded by a tough cell wall. After its hydration on stigma papillary cells, pollen tube growth starts rapidly. Massive metabolic changes are likely to be accompanied by changes in protein phosphorylation. Protein phosphorylation belongs among the most rapid post-translational modifications. To date, only Arabidopsis thaliana and tobacco (Nicotiana tabacum) mature pollen have been subjected to phosphoproteomic studies in order to identify the phosphoproteins present. In the present mini-review, Arabidopsis and tobacco datasets were compared with each other. The representation of the O-phosphorylated amino acids was compared between these two datasets, and the putative pollen-specific or pollen-abundant phosphopeptides were highlighted. Finally, the phosphorylation sites common for both Arabidopsis and tobacco phosphoproteins are listed as well as the phosphorylation motifs identified.

scholarly journals Importance of Post-Translational Modifications for Functionality of a Chloroplast-Localized Carbonic Anhydrase (CAH1) in Arabidopsis thaliana

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21021 ◽  
Author(s):  
Stefan Burén ◽  
Cristina Ortega-Villasante ◽  
Amaya Blanco-Rivero ◽  
Andrea Martínez-Bernardini ◽  
Tatiana Shutova ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Carbonic Anhydrase ◽  
Post Translational Modifications

scholarly journals Characterization of the Free and Membrane-Associated Fractions of the Thylakoid Lumen Proteome in Arabidopsis thaliana

2021 ◽  
Vol 22 (15) ◽  
pp. 8126
Author(s):  
Peter J. Gollan ◽  
Andrea Trotta ◽  
Azfar A. Bajwa ◽  
Ilaria Mancini ◽  
Eva-Mari Aro
Keyword(s):  
Arabidopsis Thaliana ◽  
Photosynthetic Electron Transport ◽  
Oxygen Evolving Complex ◽  
Ps Ii ◽  
Post Translational Modifications ◽  
Thylakoid Lumen ◽  
Novel Proteins ◽  
The Difference ◽  
Oxygen Evolving

The thylakoid lumen houses proteins that are vital for photosynthetic electron transport, including water-splitting at photosystem (PS) II and shuttling of electrons from cytochrome b6f to PSI. Other lumen proteins maintain photosynthetic activity through biogenesis and turnover of PSII complexes. Although all lumen proteins are soluble, these known details have highlighted interactions of some lumen proteins with thylakoid membranes or thylakoid-intrinsic proteins. Meanwhile, the functional details of most lumen proteins, as well as their distribution between the soluble and membrane-associated lumen fractions, remain unknown. The current study isolated the soluble free lumen (FL) and membrane-associated lumen (MAL) fractions from Arabidopsis thaliana, and used gel- and mass spectrometry-based proteomics methods to analyze the contents of each proteome. These results identified 60 lumenal proteins, and clearly distinguished the difference between the FL and MAL proteomes. The most abundant proteins in the FL fraction were involved in PSII assembly and repair, while the MAL proteome was enriched in proteins that support the oxygen-evolving complex (OEC). Novel proteins, including a new PsbP domain-containing isoform, as well as several novel post-translational modifications and N-termini, are reported, and bi-dimensional separation of the lumen proteome identified several protein oligomers in the thylakoid lumen.

scholarly journals The biogenesis of CLEL peptides involves several processing events in consecutive compartments of the secretory pathway

2018 ◽  
Author(s):  
Nils Stührwohldt ◽  
Stefan Scholl ◽  
Lisa Lang ◽  
Julia Katzenberger ◽  
Karin Schumacher ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Growth And Development ◽  
Secretory Pathway ◽  
Plant Growth And Development ◽  
Tyrosine Sulfation ◽  
Post Translational Modifications ◽  
Stringent Control ◽  
Peptide Precursors ◽  
Modified Peptides ◽  
Proline Hydroxylation

AbstractPost-translationally modified peptides are involved in many aspects of plant growth and development. The maturation of these peptides from their larger precursors is still poorly understood. We show here that the biogenesis of CLEL6 and CLEL9 peptides in Arabidopsis thaliana requires a series of processing events in consecutive compartments of the secretory pathway. Following cleavage of the signal peptide upon entry into the endoplasmic reticulum (ER), the peptide precursors are processed in the cis-Golgi by the subtilase SBT6.1. SBT6.1-mediated cleavage within the variable domain allows for continued passage of the partially processed precursors through the secretory pathway, and is a prerequisite for subsequent post-translational modifications including tyrosine sulfation and proline hydroxylation within, and proteolytic maturation after exit from the Golgi. Activation by subtilase SBT3.8 in post-Golgi compartments depends on the N-terminal aspartate of the mature peptides. Our work highlights the complexity of post-translational precursor maturation allowing for stringent control of peptide biogenesis.

scholarly journals The biogenesis of CLEL peptides involves several processing events in consecutive compartments of the secretory pathway

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Nils Stührwohldt ◽  
Stefan Scholl ◽  
Lisa Lang ◽  
Julia Katzenberger ◽  
Karin Schumacher ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Growth And Development ◽  
Secretory Pathway ◽  
Plant Growth And Development ◽  
Tyrosine Sulfation ◽  
Post Translational Modifications ◽  
Stringent Control ◽  
Peptide Precursors ◽  
Modified Peptides ◽  
Proline Hydroxylation

Post-translationally modified peptides are involved in many aspects of plant growth and development. The maturation of these peptides from their larger precursors is still poorly understood. We show here that the biogenesis of CLEL6 and CLEL9 peptides in Arabidopsis thaliana requires a series of processing events in consecutive compartments of the secretory pathway. Following cleavage of the signal peptide upon entry into the endoplasmic reticulum (ER), the peptide precursors are processed in the cis-Golgi by the subtilase SBT6.1. SBT6.1-mediated cleavage within the variable domain allows for continued passage of the partially processed precursors through the secretory pathway, and for subsequent post-translational modifications including tyrosine sulfation and proline hydroxylation within, and proteolytic maturation after exit from the Golgi. Activation by subtilases including SBT3.8 in post-Golgi compartments depends on the N-terminal aspartate of the mature peptides. Our work highlights the complexity of post-translational precursor maturation allowing for stringent control of peptide biogenesis.

scholarly journals A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots

2003 ◽  
Vol 373 (1) ◽  
pp. 289-296 ◽  
Author(s):  
Véronique SANTONI ◽  
Joëlle VINH ◽  
Delphine PFLIEGER ◽  
Nicolas SOMMERER ◽  
Christophe MAUREL
Keyword(s):  
Arabidopsis Thaliana ◽  
Plasma Membrane ◽  
Molecular Mechanisms ◽  
Direct Evidence ◽  
Two Dimensional Gel Electrophoresis ◽  
Post Translational Modifications ◽  
Ionization Time ◽  
Plasma Membrane Intrinsic Protein ◽  
Isoelectric Points ◽  
Proteomic Study

Aquaporins are channel proteins that facilitate the diffusion of water across cell membranes. The genome of Arabidopsis thaliana encodes 35 full-length aquaporin homologues. Thirteen of them belong to the plasma membrane intrinsic protein (PIP) subfamily and predominantly sit at the plasma membrane (PM). In the present work we combine separations of membrane proteins (by one- and two-dimensional gel electrophoresis) with identification by MS (matrix-assisted laser-desorption ionization–time-of-flight and electrospray-ionization tandem MS) to take an inventory of aquaporin isoforms expressed in the PM of Arabidopsis thaliana roots. Our analysis provides direct evidence for the expression of five PIPs (PIP1;1, PIP1;5, PIP2;1, PIP2;2 and PIP2;7) in the root PM and suggests the presence of at least three other PIP isoforms. In addition, we show that the same PIP isoform can be present under several forms with distinct isoelectric points. More specifically, we identify phosphorylated aquaporins in the PIP1 and PIP2 subgroups and suggest the existence of other post-translational modifications. Their identification should provide clues to reveal novel molecular mechanisms for aquaporin regulation.

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

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