Virtual 2-D map of the fungal proteome

Abstract The molecular weight and isoelectric point (pI) of the proteins plays important role in the cell. Depending upon the shape, size, and charge, protein provides its functional role in different parts of the cell. Therefore, understanding to the knowledge of their molecular weight and charges...

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Autores principales:	Tapan Kumar Mohanta, Awdhesh Kumar Mishra, Adil Khan, Abeer Hashem, Elsayed Fathi Abd-Allah, Ahmed Al-Harrasi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4516b908ce984fdcb52ecf1436d860ba
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spelling	oai:doaj.org-article:4516b908ce984fdcb52ecf1436d860ba2021-12-02T17:04:07ZVirtual 2-D map of the fungal proteome10.1038/s41598-021-86201-62045-2322https://doaj.org/article/4516b908ce984fdcb52ecf1436d860ba2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86201-6https://doaj.org/toc/2045-2322Abstract The molecular weight and isoelectric point (pI) of the proteins plays important role in the cell. Depending upon the shape, size, and charge, protein provides its functional role in different parts of the cell. Therefore, understanding to the knowledge of their molecular weight and charges is (pI) is very important. Therefore, we conducted a proteome-wide analysis of protein sequences of 689 fungal species (7.15 million protein sequences) and construct a virtual 2-D map of the fungal proteome. The analysis of the constructed map revealed the presence of a bimodal distribution of fungal proteomes. The molecular mass of individual fungal proteins ranged from 0.202 to 2546.166 kDa and the predicted isoelectric point (pI) ranged from 1.85 to 13.759 while average molecular weight of fungal proteome was 50.98 kDa. A non-ribosomal peptide synthase (RFU80400.1) found in Trichoderma arundinaceum was identified as the largest protein in the fungal kingdom. The collective fungal proteome is dominated by the presence of acidic rather than basic pI proteins and Leu is the most abundant amino acid while Cys is the least abundant amino acid. Aspergillus ustus encodes the highest percentage (76.62%) of acidic pI proteins while Nosema ceranae was found to encode the highest percentage (66.15%) of basic pI proteins. Selenocysteine and pyrrolysine amino acids were not found in any of the analysed fungal proteomes. Although the molecular weight and pI of the protein are of enormous important to understand their functional roles, the amino acid compositions of the fungal protein will enable us to understand the synonymous codon usage in the fungal kingdom. The small peptides identified during the study can provide additional biotechnological implication.Tapan Kumar MohantaAwdhesh Kumar MishraAdil KhanAbeer HashemElsayed Fathi Abd-AllahAhmed Al-HarrasiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tapan Kumar Mohanta Awdhesh Kumar Mishra Adil Khan Abeer Hashem Elsayed Fathi Abd-Allah Ahmed Al-Harrasi Virtual 2-D map of the fungal proteome
description	Abstract The molecular weight and isoelectric point (pI) of the proteins plays important role in the cell. Depending upon the shape, size, and charge, protein provides its functional role in different parts of the cell. Therefore, understanding to the knowledge of their molecular weight and charges is (pI) is very important. Therefore, we conducted a proteome-wide analysis of protein sequences of 689 fungal species (7.15 million protein sequences) and construct a virtual 2-D map of the fungal proteome. The analysis of the constructed map revealed the presence of a bimodal distribution of fungal proteomes. The molecular mass of individual fungal proteins ranged from 0.202 to 2546.166 kDa and the predicted isoelectric point (pI) ranged from 1.85 to 13.759 while average molecular weight of fungal proteome was 50.98 kDa. A non-ribosomal peptide synthase (RFU80400.1) found in Trichoderma arundinaceum was identified as the largest protein in the fungal kingdom. The collective fungal proteome is dominated by the presence of acidic rather than basic pI proteins and Leu is the most abundant amino acid while Cys is the least abundant amino acid. Aspergillus ustus encodes the highest percentage (76.62%) of acidic pI proteins while Nosema ceranae was found to encode the highest percentage (66.15%) of basic pI proteins. Selenocysteine and pyrrolysine amino acids were not found in any of the analysed fungal proteomes. Although the molecular weight and pI of the protein are of enormous important to understand their functional roles, the amino acid compositions of the fungal protein will enable us to understand the synonymous codon usage in the fungal kingdom. The small peptides identified during the study can provide additional biotechnological implication.
format	article
author	Tapan Kumar Mohanta Awdhesh Kumar Mishra Adil Khan Abeer Hashem Elsayed Fathi Abd-Allah Ahmed Al-Harrasi
author_facet	Tapan Kumar Mohanta Awdhesh Kumar Mishra Adil Khan Abeer Hashem Elsayed Fathi Abd-Allah Ahmed Al-Harrasi
author_sort	Tapan Kumar Mohanta
title	Virtual 2-D map of the fungal proteome
title_short	Virtual 2-D map of the fungal proteome
title_full	Virtual 2-D map of the fungal proteome
title_fullStr	Virtual 2-D map of the fungal proteome
title_full_unstemmed	Virtual 2-D map of the fungal proteome
title_sort	virtual 2-d map of the fungal proteome
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4516b908ce984fdcb52ecf1436d860ba
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Virtual 2-D map of the fungal proteome

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