scholarly journals In silico Identification and Analysis of Iron (Fe) Transporters in Various Plant Species

2020 ◽  
pp. 14-23
Author(s):  
Akula Dinesh ◽  
Ramya Rathod ◽  
M. Sreedhar
Keyword(s):  
Molecular Weight ◽  
Plant Species ◽  
Cellular Localization ◽  
Sequence Length ◽  
Theoretical Knowledge ◽  
Conserved Residues ◽  
Fe Content ◽  
Transgenic Breeding ◽  
In Silico Identification ◽  
Molecular Manipulation

In plants, Iron is an important micronutrient which is required for various processes like photosynthesis, respiration and for balanced redox potential. Iron has a significant role in human nutrition. Therefore, increasing the Fe content of economical parts through conventional, Molecular and/or Transgenic breeding will have dramatic impact on human health. Therefore, this study was aimed to identify and characterize homologues of OsIRT1, OsIRT2, OsVIT1, OsYSL2, OsYSL15 and OsYSL18 in 21 different plant species. The study revealed that, a total of 51 putative Fe transporter proteins homologues were identified which could be characterized with 555 to770 amino acids sequence length with 61 to 84.8 kDa molecular weight and pI of 8.2 to 9.4 having basic nature with 9 to15 TMD with an average of 13 TMDs. The sub-cellular localization of putative Fe transporters was predicted as the plasma membrane and all the identified Fe homologues contained oligopeptide transporter (OPT) domain proteins which play a significant to role in Fe transport and homeostasis. Further, the analysis led to identification of highly conserved residues in the putative Fe sequences which could be used as potential motif signatures in identification of new Fe transporter. The interactome analysis for oryza sativa OsYSL15 transporter showed putative interaction with NAS2, NAS1, DMAS1, OsJ_32857, IRT1, IRO2, IDEF1, IRT2, IDI2 which are found to be directly involved in Fe transport from roots to grain. This study, elucidates the valuable theoretical knowledge about the Fe genes, protein features and assist in molecular manipulation of Fe transporters in various plants for developing high Fe in economical part.

Differences in solubility parameters and susceptibility to salting-out between softwood and hardwood lignosulfonates

Holzforschung ◽  
2016 ◽  
Vol 70 (11) ◽  
pp. 1015-1021 ◽  
Author(s):  
Bernt O. Myrvold
Keyword(s):  
Molecular Weight ◽  
Salt Tolerance ◽  
Plant Species ◽  
Post Treatment ◽  
Solubility Parameters ◽  
Minor Effect ◽  
Hofmeister Series ◽  
Salt Tolerant ◽  
Salting Out ◽  
A Minor

Abstract The salting-out of lignosulfonates (LSs) follows the Hofmeister series, but different LSs show different susceptibility to salting-out. By comparing results for a large number of LSs from different plant species, pulping conditions, and post-treatment of the LS, it was found that the salting-out concentration for different LSs is mainly due to differences in the plant species with guaiacyl LS being much more salt-tolerant than guaiacyl-syringyl LS. The pulping conditions have only a minor effect on the salt tolerance of the different LSs. Post-treatment that increases the molecular weight or reduces the sulfonation also reduces the salt tolerance.

scholarly journals Sea urchin (Anthocidaris crassispina) egg zinc-binding protein. Cellular localization, purification and characterization

1983 ◽  
Vol 211 (1) ◽  
pp. 109-118 ◽  
Author(s):  
H Ohtake ◽  
T Suyemitsu ◽  
M Koga
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Sea Urchin ◽  
Cellular Localization ◽  
Binding Protein ◽  
Gel Permeation Chromatography ◽  
Total Amino Acid ◽  
Amino Acid Residues ◽  
Gel Permeation ◽  
Anthocidaris Crassispina

Gel-filtration analysis of cytosol fraction obtained from unfertilized sea-urchin (Anthocidaris crassispina) eggs on Sephadex G-75 revealed the presence of two Zn-binding-protein fractions. The major Zn-binding protein fraction had a low molecular weight and a low absorbance at 280 nm, properties similar to those of the metallothionein found in the regenerating rat liver. These fractions were further purified by DEAE-cellulose and Sephadex G-50 chromatography. Homogeneity of the Zn-binding protein was judged by polyacrylamide-disc-gel electrophoresis and gel-permeation chromatography in the presence of 6 M-guanidinium chloride. The molecular weight determined by gel-permeation chromatography was 3900. This value is in good agreement with the minimum molecular weight calculated from the amino acid composition, which was 3655. Zn-binding protein is composed of 36 amino acid residues and the distinctive features include an extremely high content of cysteine, which accounted for one-third of the total amino acid residues, and a complete absence of aromatic amino acids, as well as of methionine, histidine and arginine. Zn-binding protein contained 4.1 g-atoms of zinc per mol and a trace of cadmium, but no copper, iron or calcium. The molar ratio of reactive thiol groups to metal ion was calculated to be 2.73:1. Possible roles of this Zn-binding protein in the homoeostasis of zinc in unfertilized sea-urchin eggs are discussed.

A Rapid and Economical Method for Low Molecular Weight RNA Isolation from a Wide Variety of Plant Species

2013 ◽  
Vol 77 (7) ◽  
pp. 1599-1601 ◽  
Author(s):  
Zewei AN ◽  
Yachao LI ◽  
Lili XIE ◽  
Qilin ZHAI ◽  
Huasun HUANG
Keyword(s):  
Molecular Weight ◽  
Plant Species ◽  
Rna Isolation ◽  
Low Molecular Weight ◽  
Economical Method

scholarly journals Progress and challenges in the synthesis of sequence controlled polysaccharides

2021 ◽  
Vol 17 ◽  
pp. 1981-2025
Author(s):  
Giulio Fittolani ◽  
Theodore Tyrikos-Ergas ◽  
Denisa Vargová ◽  
Manishkumar A Chaube ◽  
Martina Delbianco
Keyword(s):  
Molecular Weight ◽  
Chemical Synthesis ◽  
Weight Distribution ◽  
Biological Properties ◽  
Sequence Length ◽  
Narrow Molecular Weight Distribution ◽  
Full Control ◽  
Synthetic Approaches ◽  
Enzymatic Methods ◽  
Structure Properties

The sequence, length and substitution of a polysaccharide influence its physical and biological properties. Thus, sequence controlled polysaccharides are important targets to establish structure–properties correlations. Polymerization techniques and enzymatic methods have been optimized to obtain samples with well-defined substitution patterns and narrow molecular weight distribution. Chemical synthesis has granted access to polysaccharides with full control over the length. Here, we review the progress towards the synthesis of well-defined polysaccharides. For each class of polysaccharides, we discuss the available synthetic approaches and their current limitations.

scholarly journals Global Characterization of XRN 5′-3′ Exoribonucleases and Their Responses to Environmental Stresses in Plants

Diversity ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 612
Author(s):  
Weimeng Song ◽  
Yanjie Li ◽  
Yue Niu ◽  
You Wu ◽  
Yan Bao ◽  
...  
Keyword(s):  
Plant Species ◽  
Cellular Localization ◽  
Expression Patterns ◽  
Environmental Stresses ◽  
Transcriptional Level ◽  
Element Analysis ◽  
Nuclear Localization Signals ◽  
Conserved Sequence ◽  
Response Diversity ◽  
Eukaryotic Organisms

The XRN family of 5′-3′ Exoribonucleases is functionally conserved in eukaryotic organisms. However, the molecular evolution of XRN proteins in plants and their functions in plant response to environment stresses remain largely unexplored. In this study, we identified 23 XRN proteins in 6 representative plant species. Polygenetic analysis revealed that XRN2 was Arabidopsis-specific among these species, and additional branches outside the clades of XRN3 and XRN4 proteins, which we named as XRN5, were found in rice, maize, and soybean. However, XRN5 in soybean lost their entire 5′-3′ XRN Exoribonuclease domain. Protein conserved sequence analysis showed that XRN3/XRN2 contained potential bipartite nuclear-localization signals (NLS) while all the XRN4 proteins lost their second KR/RR motif of NLS, potentially leading to their cytoplasm localization. SIXRN3-2 contained one mutation in this second KR/RR motif, which may change their sub-cellular localization. The promoter cis-element analysis indicated that these XRN genes responded to multiple stresses and plant hormones diversely at transcriptional level. Finally, transcriptomic analysis suggested that OsXRN3 and ZmXRN3-1 were induced by low temperature, SIXRN4 and ZmXRN4 was inhibited by heat shock, and OsXRN5 and GmXRN5-2 were repressed by drought. However, in general, the expression patterns revealed the response diversity of XRNs to environment stimuli in different plant species. Taken together, this study characterized 23 XRNs with NLS variation that contributed to their sub-cellular localization and provided an overview of the XRNs response diversity to multiple environmental stresses, suggesting that XRNs could be used as potential gene editing candidates for precise stress-tolerant crop breeding.

scholarly journals Immunovisualization of high (HK) and low (LK) molecular weight kininogens on isolated human neutrophils

Blood ◽  
1992 ◽  
Vol 79 (3) ◽  
pp. 754-759
Author(s):  
CD Figueroa ◽  
LM Henderson ◽  
J Kaufmann ◽  
RA De La Cadena ◽  
RW Colman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cellular Localization ◽  
Confocal Scanning Laser Microscopy ◽  
Human Neutrophils ◽  
Low Molecular Weight ◽  
High Molecular Weight Kininogen ◽  
Confocal Scanning ◽  
Silver Staining Method ◽  
Confocal Scanning Laser

An immunocytochemical study was performed to examine the cellular localization and the subcellular distribution of kininogens in human blood cells. Kininogens were visualised using the immunogold-silver staining method and confocal scanning laser microscopy. We confirmed the existence of high molecular weight kininogen in human neutrophils and describe for the first time the presence of low molecular weight kininogen on these cells. Both high and low molecular weight kininogens were restricted to the neutrophils where they localized as clusters of immunogold particles on the cell membrane. No labeling was observed intracellularly in organelles such as mitochondria, endoplasmic reticulum, and azurophilic or specific granules after permeabilization of the neutrophils with Triton X-100, a procedure that permitted the visualization of elastase in the azurophilic granules. Clusters of high molecular weight kininogen molecules attached to the neutrophil surface could serve as receptors for plasma kallikrein and/or be the source of substrate for a discrete and circumscribed formation of kinins that may in turn facilitate the local diapedesis of neutrophils and the transudation of plasma constituents during acute inflammation.

scholarly journals The Molecular Mass and Isoelectric Point of Plant Proteomes

2019 ◽  
Author(s):  
Tapan Kumar Kumar Mohanta ◽  
Abdulatif Khan ◽  
Abeer Hashem ◽  
Elsayed Fathi Abd_Allah ◽  
Ahmed Al-Harrasi
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Molecular Mass ◽  
Plant Species ◽  
Isoelectric Point ◽  
Polyketide Synthase ◽  
Type I ◽  
Plant Proteins ◽  
Higher Plant

Abstract Background Cell contain diverse array of proteins with different molecular weight and isoelectric point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and isoelectric point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.

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