Identification and Characterization of Plant Membrane Proteins Using ARAMEMNON

Schwacke, Rainer; Flügge, Ulf‐Ingo

doi:10.1007/978-1-4939-7411-5_17

Cited by 12 publications

(7 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To assess the membrane organization of the atMB-TFs, we computationally evaluated the positions relative to the TFFD of the TMDs and their membrane topology. Similar to the study of Yao et al (2017) , the TFFD position within the MB-TF and the TMD position and orientation were retrieved from the PlnTFDB v5.0 ( Riaño-Pachón et al, 2007 ) and the TMHMM predictor ( Krogh et al, 2001 ) and Aramemnon tool that integrates 18 different TMD-predicting algorithms ( Schwacke et al, 2003 ; Schwacke and Flügge, 2018 ), respectively ( Table 1 ). Based on the TMD position, we distinguished three atMB-TF groups with the TMD (i) on the C-terminal side of the TFFD (60.3%) ( Figures 1A,B ), (ii) on the N-terminal side of the TFFD (23.8%) ( Figures 1C,D ), and (iii) overlapping with the TFFD (15.9%) ( Figure 1E ).…”

Section: Membrane Targeting and Topology Of Atmb-tfsmentioning

confidence: 99%

Proteolytic Activation of Plant Membrane-Bound Transcription Factors

2022

View full text Add to dashboard Cite

Due to the presence of a transmembrane domain, the subcellular mobility plan of membrane-bound or membrane-tethered transcription factors (MB-TFs) differs from that of their cytosolic counterparts. The MB-TFs are mostly locked in (sub)cellular membranes, until they are released by a proteolytic cleavage event or when the transmembrane domain (TMD) is omitted from the transcript due to alternative splicing. Here, we review the current knowledge on the proteolytic activation mechanisms of MB-TFs in plants, with a particular focus on regulated intramembrane proteolysis (RIP), and discuss the analogy with the proteolytic cleavage of MB-TFs in animal systems. We present a comprehensive inventory of all known and predicted MB-TFs in the model plant Arabidopsis thaliana and examine their experimentally determined or anticipated subcellular localizations and membrane topologies. We predict proteolytically activated MB-TFs by the mapping of protease recognition sequences and structural features that facilitate RIP in and around the TMD, based on data from metazoan intramembrane proteases. Finally, the MB-TF functions in plant responses to environmental stresses and in plant development are considered and novel functions for still uncharacterized MB-TFs are forecasted by means of a regulatory network-based approach.

show abstract

Section: Membrane Targeting and Topology Of Atmb-tfsmentioning

confidence: 99%

Proteolytic Activation of Plant Membrane-Bound Transcription Factors

2022

View full text Add to dashboard Cite

show abstract

“…Mature MSL1 was defined as the protein remaining after cleavage of the mitochondrial transit peptide at Phe‐79 (RAF↓SS; Lee et al., ), while mature MSL2 and MSL3 were defined as the protein remaining after cleavage of the predicted chloroplast transit peptide at Arg‐75 (AFR↓CH) and Arg‐70 (SSR↓CN) respectively (Haswell & Meyerowitz, ). Transmembrane domains and overall topology were predicted with Aramemnon (Schwacke & Flügge, ). Amino acid sequences were aligned using Clustal Omega 1.2.4 and default settings (Sievers & Higgins, ).…”

Section: Methodsmentioning

confidence: 99%

Genetic and physical interactions between the organellar mechanosensitive ion channel homologs MSL1, MSL2, and MSL3 reveal a role for inter‐organellar communication in plant development

et al. 2019

View full text Add to dashboard Cite

Plant development requires communication on many levels, including between cells and between organelles within a cell. For example, mitochondria and plastids have been proposed to be sensors of environmental stress and to coordinate their responses. Here we present evidence for communication between mitochondria and chloroplasts during leaf and root development, based on genetic and physical interactions between three M echanosensitive channel of S mall conductance‐ L ike ( MSL ) proteins from Arabidopsis thaliana . MSL proteins are Arabidopsis homologs of the bacterial M echano s ensitive c hannel of S mall conductance (MscS), which relieves cellular osmotic pressure to protect against lysis during hypoosmotic shock. MSL 1 localizes to the inner mitochondrial membrane, while MSL 2 and MSL 3 localize to the inner plastid membrane and are required to maintain plastid osmotic homeostasis during normal growth and development. In this study, we characterized the phenotypic effect of a genetic lesion in MSL 1 , both in wild type and in msl2 msl3 mutant backgrounds. msl1 single mutants appear wild type for all phenotypes examined. The characteristic leaf rumpling in msl2 msl3 double mutants was exacerbated in the msl1 msl2 msl3 triple mutant. However, the introduction of the msl1 lesion into the msl2 msl3 mutant background suppressed other msl2 msl3 mutant phenotypes, including ectopic callus formation, accumulation of superoxide and hydrogen peroxide in the shoot apical meristem, decreased root length, and reduced number of lateral roots. All these phenotypes could be recovered by molecular complementation with a transgene containing a wild type version of MSL 1 . In yeast‐based interaction studies, MSL 1 interacted with itself, but not with MSL 2 or MSL 3. These results establish that the abnormalities observed in msl2 msl3 double mutants is partially dependent on the presence of functional MSL 1 and suggest a possible role for communication between plastid and mitochondria in seedling development.

show abstract

“…Mature MSL1 was defined as the protein remaining after cleavage of the mitochondrial transit peptide at Phe-79 (RAF↓SS; (Lee et al, 2016)), while mature MSL2 and MSL3 were defined as the protein remaining after cleavage of the predicted chloroplast transit peptide at Arg-75 (AFR↓CH) and Arg-70 (SSR↓CN) respectively (Haswell and Meyerowitz, 2006). Transmembrane domains and overall topology were predicted with Aramemnon (Schwacke and Flügge, 2018). Amino acid sequences were aligned using Clustal Omega 1.2.4 and default settings (Sievers and Higgins, 2018).…”

Section: Methodsmentioning

confidence: 99%

Genetic and physical interactions between the organellar mechanosensitive ion channel homologs MSL1, MSL2, and MSL3 reveal a role for inter-organellar communication in plant development

Lee

Wilson

Richardson

et al. 2018

Preprint

View full text Add to dashboard Cite

8 USA 9 10 keywords: mechanosensitive channel, Arabidopsis, mitochondria, chloroplast, reactive oxygen 11 species 12 13 2 ABSTRACT 14 15 Plant development requires communication on many levels, including between cells and between 16 organelles within a cell. For example, mitochondria and plastids have been proposed to be sensors 17 of environmental stress and to coordinate their responses. Here we present evidence for 18 communication between mitochondria and chloroplasts during leaf and root development, based 19 on genetic and physical interactions between three Mechanosensitive channels of Small 20 conductance-Like (MSL) proteins from Arabidopsis thaliana. MSL proteins are Arabidopsis 21 homologs of the bacterial Mechanosensitive channel of Small conductance (MscS), which relieves 22 cellular osmotic pressure to protect against lysis during hypoosmotic shock. MSL1 localizes to the 23 inner mitochondrial membrane, while MSL2 and MSL3 localize to the inner plastid membrane 24and are required to maintain plastid osmotic homeostasis during normal growth and development. 25In this study, we characterized the phenotypic effect of a genetic lesion in MSL1, both in wild type 26 and in msl2 msl3 mutant backgrounds. msl1 single mutants appear wild type for all phenotypes 27 examined. The characteristic leaf rumpling in msl2 msl3 double mutants was exacerbated in the 28 msl1 msl2 msl3 triple mutant. However, the introduction of the msl1 lesion into the msl2 msl3 29 mutant background suppressed other msl2 msl3 mutant phenotypes, including ectopic callus 30 formation, accumulation of superoxide and hydrogen peroxide in the shoot apical meristem, 31 decreased root length, and reduced number of lateral roots. All these phenotypes could be 32 recovered by molecular complementation with a transgene containing a wild type version of MSL1. 33In yeast-based interaction studies, MSL1 interacted with itself, but not with MSL2 or MSL3. These 34 results establish that the abnormalities observed in msl2 msl3 double mutants is partially dependent 35 on the presence of functional MSL1 and suggest a possible role for communication between plastid 36 and mitochondria in seedling development.37 38 39 40 Plastids and mitochondria are found in almost every plant cell and are involved in all aspects of 41 plant biology. In plants, as in animals, mitochondria are involved in multiple cellular processes, 42 including cellular respiration and co-enzyme synthesis (Schertl and Braun, 2014; Rébeillé et al., 43 2007). Plastids are responsible for photosynthesis and a range of other biosynthetic reactions-44 including the production of starch, some amino acids, fatty acids and lipids, pigments, hormones 45 and volatiles (Neuhaus:2000eh; Rolland et al., 2018). Some plastids play a unique role in plant 46 biology: amyloplasts in the root tip and the shoot endodermis are essential for gravity response 47 (Toyota:2013fe; Su et al., 2017). A recent report argues that plastids of the leaf epidermis can serve 48 as stress sensors (Beltrán et al., 2018). Whi...

show abstract

Identification and Characterization of Plant Membrane Proteins Using ARAMEMNON

Cited by 12 publications

References 15 publications

Proteolytic Activation of Plant Membrane-Bound Transcription Factors

Proteolytic Activation of Plant Membrane-Bound Transcription Factors

Genetic and physical interactions between the organellar mechanosensitive ion channel homologs MSL1, MSL2, and MSL3 reveal a role for inter‐organellar communication in plant development

Genetic and physical interactions between the organellar mechanosensitive ion channel homologs MSL1, MSL2, and MSL3 reveal a role for inter-organellar communication in plant development

Contact Info

Product

Resources

About