Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)
Transferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harb...
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2022-12-01
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author | Jun Cao |
author_facet | Jun Cao |
author_sort | Jun Cao |
collection | DOAJ |
description | Transferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harbored obvious N-lobe and C-lobe domains. The tissue-specific expression pattern showed that the transcript was detected in a variety of tissues, with the highest signal in liver. Moreover, <i>Streptococcus iniae</i> pathogen stimulation can increase the expression level of this transcript, implying important immune properties for organisms. Next, N-lobes and C-lobes were obtained from 45 fish species. The phylogenetic tree showed that N-lobes and C-lobes were in two different evolutionary branches, and they had different motif composition. Functional divergence indicated a higher evolutionary rate or site-specific alteration among the N-lobe and C-lobe groups. <i>Ka</i>/<i>Ks</i> value of C-lobe group was relatively higher than that of N-lobe group, indicating a faster change rate of C-lobe sequences in evolution. Moreover, some sites experiencing positive selection were also found, which may be involved in the iron- or anion-binding, pathogen resistance and diversification of transferrin protein. Differential iron-binding activity was also detected between N-lobe and C-lobe of Amur stickleback transferrin protein with Chrome Azurol S assay. Compared with the C-lobe, the N-lobe showed stronger growth inhibitory activity of <i>Escherichia coli</i>, implying their potential antibacterial properties. This study will give a reference for subsequent research of transferrin proteins. |
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spelling | doaj.art-b5143ebc2be944789e63d64a10d6dcca2023-11-24T12:50:04ZengMDPI AGAnimals2076-26152022-12-011224345810.3390/ani12243458Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback)Jun Cao0School of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaTransferrin is an important iron-binding glycosylated protein and plays key roles in iron-binding and immune response. Here, a 2037-bp open reading frame was obtained from our previous transcriptome sequencing data of Amur stickleback, which encoded a 679 amino acid putative transferrin protein harbored obvious N-lobe and C-lobe domains. The tissue-specific expression pattern showed that the transcript was detected in a variety of tissues, with the highest signal in liver. Moreover, <i>Streptococcus iniae</i> pathogen stimulation can increase the expression level of this transcript, implying important immune properties for organisms. Next, N-lobes and C-lobes were obtained from 45 fish species. The phylogenetic tree showed that N-lobes and C-lobes were in two different evolutionary branches, and they had different motif composition. Functional divergence indicated a higher evolutionary rate or site-specific alteration among the N-lobe and C-lobe groups. <i>Ka</i>/<i>Ks</i> value of C-lobe group was relatively higher than that of N-lobe group, indicating a faster change rate of C-lobe sequences in evolution. Moreover, some sites experiencing positive selection were also found, which may be involved in the iron- or anion-binding, pathogen resistance and diversification of transferrin protein. Differential iron-binding activity was also detected between N-lobe and C-lobe of Amur stickleback transferrin protein with Chrome Azurol S assay. Compared with the C-lobe, the N-lobe showed stronger growth inhibitory activity of <i>Escherichia coli</i>, implying their potential antibacterial properties. This study will give a reference for subsequent research of transferrin proteins.https://www.mdpi.com/2076-2615/12/24/3458immune responseiron-bindingantibacterial propertymolecular evolutionfunctional divergenceselection pressure |
spellingShingle | Jun Cao Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) Animals immune response iron-binding antibacterial property molecular evolution functional divergence selection pressure |
title | Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) |
title_full | Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) |
title_fullStr | Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) |
title_full_unstemmed | Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) |
title_short | Functional Divergence of the N-Lobe and C-Lobe of <i>Transferrin</i> Gene in <i>Pungitius sinensis</i> (Amur Stickleback) |
title_sort | functional divergence of the n lobe and c lobe of i transferrin i gene in i pungitius sinensis i amur stickleback |
topic | immune response iron-binding antibacterial property molecular evolution functional divergence selection pressure |
url | https://www.mdpi.com/2076-2615/12/24/3458 |
work_keys_str_mv | AT juncao functionaldivergenceofthenlobeandclobeofitransferrinigeneinipungitiussinensisiamurstickleback |