In Silico Analysis of Thioredoxins and Glutaredoxins
Thioredoxins (TRXs) and glutaredoxins (GRXs) are ubiquitous small redox proteins belonging to the thioredoxin (TRX) superfamily. They regulate several cellular functions via mediating a dithiol/disulphide exchange in target proteins. Thioredoxins have been classified into several subgroups based on...
Published in: | Journal of Plant Biochemistry and Biotechnology |
---|---|
Main Authors: | , , |
Format: | Text |
Language: | unknown |
Published: |
Digital Commons @ East Tennessee State University
2005
|
Subjects: | |
Online Access: | https://dc.etsu.edu/etsu-works/18470 https://doi.org/10.1007/bf03263239 |
id |
fteasttennesseeu:oai:dc.etsu.edu:etsu-works-19736 |
---|---|
record_format |
openpolar |
spelling |
fteasttennesseeu:oai:dc.etsu.edu:etsu-works-19736 2023-07-30T04:06:36+02:00 In Silico Analysis of Thioredoxins and Glutaredoxins Srivastava, Renu Kitambi, Satish Srinivas Goyal, Arun 2005-01-01T08:00:00Z https://dc.etsu.edu/etsu-works/18470 https://doi.org/10.1007/bf03263239 unknown Digital Commons @ East Tennessee State University https://dc.etsu.edu/etsu-works/18470 doi:10.1007/bf03263239 https://doi.org/10.1007/bf03263239 ETSU Faculty Works glutaredoxin phylogenetic redox proteins thioredoxin text 2005 fteasttennesseeu https://doi.org/10.1007/bf03263239 2023-07-15T18:46:42Z Thioredoxins (TRXs) and glutaredoxins (GRXs) are ubiquitous small redox proteins belonging to the thioredoxin (TRX) superfamily. They regulate several cellular functions via mediating a dithiol/disulphide exchange in target proteins. Thioredoxins have been classified into several subgroups based on their structural homologs. In an attempt to identify thioredoxin proteins which have not been characterized, an EST database survey of Lycopersicon esculentum, Glycine max, Helianthus annus, Secale cereale, Solanum tuberosum, Apis mellifera ligustica, Oncorhynchus mykiss, Salmo salar, and whole genome survey for Drosophila melanogaster, Rattus norvegicus and Caenorhabditis briggsae was performed. Several glutaredoxin and glutaredoxin-like proteins from Ricinus communis, Vercinia fordii, Lycopersicon esculentum, Tilia platyphyllos, Populus tremuloides, Triticum aestivum and Oryza sativa were also characterized. The deduced amino acid sequences were aligned and phylogenetic trees were constructed to determine the consensus sequences and for establishing interrelationships amongst the new and established thioredoxin and glutaredoxins. Based on the alignments, proteins were designated to their respective classes and subcellular localization predictions were used to predict their possible site of actions. In silico analysis has identified several new thioredoxins, glutaredoxins and related proteins and provided insight into their evolutionary relationships. Text Salmo salar Digital Commons @ East Tennessee State University Journal of Plant Biochemistry and Biotechnology 14 2 121 126 |
institution |
Open Polar |
collection |
Digital Commons @ East Tennessee State University |
op_collection_id |
fteasttennesseeu |
language |
unknown |
topic |
glutaredoxin phylogenetic redox proteins thioredoxin |
spellingShingle |
glutaredoxin phylogenetic redox proteins thioredoxin Srivastava, Renu Kitambi, Satish Srinivas Goyal, Arun In Silico Analysis of Thioredoxins and Glutaredoxins |
topic_facet |
glutaredoxin phylogenetic redox proteins thioredoxin |
description |
Thioredoxins (TRXs) and glutaredoxins (GRXs) are ubiquitous small redox proteins belonging to the thioredoxin (TRX) superfamily. They regulate several cellular functions via mediating a dithiol/disulphide exchange in target proteins. Thioredoxins have been classified into several subgroups based on their structural homologs. In an attempt to identify thioredoxin proteins which have not been characterized, an EST database survey of Lycopersicon esculentum, Glycine max, Helianthus annus, Secale cereale, Solanum tuberosum, Apis mellifera ligustica, Oncorhynchus mykiss, Salmo salar, and whole genome survey for Drosophila melanogaster, Rattus norvegicus and Caenorhabditis briggsae was performed. Several glutaredoxin and glutaredoxin-like proteins from Ricinus communis, Vercinia fordii, Lycopersicon esculentum, Tilia platyphyllos, Populus tremuloides, Triticum aestivum and Oryza sativa were also characterized. The deduced amino acid sequences were aligned and phylogenetic trees were constructed to determine the consensus sequences and for establishing interrelationships amongst the new and established thioredoxin and glutaredoxins. Based on the alignments, proteins were designated to their respective classes and subcellular localization predictions were used to predict their possible site of actions. In silico analysis has identified several new thioredoxins, glutaredoxins and related proteins and provided insight into their evolutionary relationships. |
format |
Text |
author |
Srivastava, Renu Kitambi, Satish Srinivas Goyal, Arun |
author_facet |
Srivastava, Renu Kitambi, Satish Srinivas Goyal, Arun |
author_sort |
Srivastava, Renu |
title |
In Silico Analysis of Thioredoxins and Glutaredoxins |
title_short |
In Silico Analysis of Thioredoxins and Glutaredoxins |
title_full |
In Silico Analysis of Thioredoxins and Glutaredoxins |
title_fullStr |
In Silico Analysis of Thioredoxins and Glutaredoxins |
title_full_unstemmed |
In Silico Analysis of Thioredoxins and Glutaredoxins |
title_sort |
in silico analysis of thioredoxins and glutaredoxins |
publisher |
Digital Commons @ East Tennessee State University |
publishDate |
2005 |
url |
https://dc.etsu.edu/etsu-works/18470 https://doi.org/10.1007/bf03263239 |
genre |
Salmo salar |
genre_facet |
Salmo salar |
op_source |
ETSU Faculty Works |
op_relation |
https://dc.etsu.edu/etsu-works/18470 doi:10.1007/bf03263239 https://doi.org/10.1007/bf03263239 |
op_doi |
https://doi.org/10.1007/bf03263239 |
container_title |
Journal of Plant Biochemistry and Biotechnology |
container_volume |
14 |
container_issue |
2 |
container_start_page |
121 |
op_container_end_page |
126 |
_version_ |
1772819295564201984 |