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The molecular mass and isoelectric point of plant proteomes

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 we...

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Autores principales: Mohanta, Tapan Kumar, Khan, Abdullatif, Hashem, Abeer, Abd_Allah, Elsayed Fathi, Al-Harrasi, Ahmed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6681478/
https://www.ncbi.nlm.nih.gov/pubmed/31382875
http://dx.doi.org/10.1186/s12864-019-5983-8
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author Mohanta, Tapan Kumar
Khan, Abdullatif
Hashem, Abeer
Abd_Allah, Elsayed Fathi
Al-Harrasi, Ahmed
author_facet Mohanta, Tapan Kumar
Khan, Abdullatif
Hashem, Abeer
Abd_Allah, Elsayed Fathi
Al-Harrasi, Ahmed
author_sort Mohanta, Tapan Kumar
collection PubMed
description 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-019-5983-8) contains supplementary material, which is available to authorized users.
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spelling pubmed-66814782019-08-07 The molecular mass and isoelectric point of plant proteomes Mohanta, Tapan Kumar Khan, Abdullatif Hashem, Abeer Abd_Allah, Elsayed Fathi Al-Harrasi, Ahmed BMC Genomics Research Article 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-019-5983-8) contains supplementary material, which is available to authorized users. BioMed Central 2019-08-05 /pmc/articles/PMC6681478/ /pubmed/31382875 http://dx.doi.org/10.1186/s12864-019-5983-8 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Mohanta, Tapan Kumar
Khan, Abdullatif
Hashem, Abeer
Abd_Allah, Elsayed Fathi
Al-Harrasi, Ahmed
The molecular mass and isoelectric point of plant proteomes
title The molecular mass and isoelectric point of plant proteomes
title_full The molecular mass and isoelectric point of plant proteomes
title_fullStr The molecular mass and isoelectric point of plant proteomes
title_full_unstemmed The molecular mass and isoelectric point of plant proteomes
title_short The molecular mass and isoelectric point of plant proteomes
title_sort molecular mass and isoelectric point of plant proteomes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6681478/
https://www.ncbi.nlm.nih.gov/pubmed/31382875
http://dx.doi.org/10.1186/s12864-019-5983-8
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