Genome-wide exploration of sugar transporter (sweet) family proteins in Fabaceae for Sustainable protein and carbon source

Sugar transporter proteins (STPs) are membrane proteins required for sugar transport throughout cellular membranes. They plays an imperative role in sugar transmission across the plant and determinants of crop yield. However, the analysis of these important STPs Sugars Will Eventually be Exported Tr...

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Published in:PloS one Vol. 17; no. 5; p. e0268154
Main Authors: Singh, Nisha, Ujinwal, Megha, Langyan, Sapna, Sayyed, R Z, El Enshasy, Hesham Ali, Kenawy, Ahmed A
Format: Journal Article
Language:English
Published: United States Public Library of Science 13-05-2022
Public Library of Science (PLoS)
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Summary:Sugar transporter proteins (STPs) are membrane proteins required for sugar transport throughout cellular membranes. They plays an imperative role in sugar transmission across the plant and determinants of crop yield. However, the analysis of these important STPs Sugars Will Eventually be Exported Transporters (SWEET) family in legumes is still not well-documented and remains unclear. Therefore, the in-silico analysis of STPs has been performed to unravel their cellular, molecular, and structural composition in legume species. This study conducted a systematic search for STPs in Cajanus cajan using the Blastp algorithm to understand its molecular basis. Here, we performed a comprehensive analysis of 155 identified SWEET proteins across 12 legumes species, namely (Cajanus cajan, Glycine max, Vigna radiate, Vigna angularis, Medicago truncatula, Lupinus angustifolius, Glycine soja, Spatholobus suberectus, Cicer arietinum, Arachis ipaensis, Arachis hypogaea, Arachis duranensis). The amino acid composition and motif analysis revealed that SWEET proteins are rich in essential amino acids such as leucine, valine, isoleucine, phenylalanine, and serine while less profuse in glutamine, tryptophan, cysteine, and histidine. A total of four main conserved motifs of SWEET proteins are also highly abundant in these amino acids. The present study deciphered the details on primary physicochemical properties, secondary, tertiary structure, and phylogenetic analysis of SWEETs protein. Majorities of SWEET proteins (72.26%) are in stable form with an average instability index of 36.5%, and it comprises a higher fraction of positively charged amino acid Arg + Lys residues. Secondary structure analysis shown that these proteins are richer in alpha-helix (40%) than extended strand (30%) and random coil (25%), respectively. Furthermore, to infer their mechanism at a structural and functional level which play an essential roles in growth, development, and stress responses. This study will be useful to examine photosynthetic productivity, embryo sugar content, seed quality, and yield enhancement in Fabaceae for a sustainable source of essential amino acids and carbon source.
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Competing Interests: The authors have declared that no competing interests exist.
These authors also contributed equally to this work
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0268154