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Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis

BACKGROUND: Ribosome biogenesis is the process of assembling ribosome complexes that regulate cell proliferation and differentiation with potential regulatory effects on development. Many factors regulate ribosome biological processes. Nin one binding protein (Nob1) has received widespread attention...

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Autores principales: Zhou, Huan, Yuan, Wang, Lei, Weiqiang, Zhou, Taoxun, Qin, Peixi, Zhang, Biying, Hu, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10623843/
https://www.ncbi.nlm.nih.gov/pubmed/37924155
http://dx.doi.org/10.1186/s13071-023-05940-9
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author Zhou, Huan
Yuan, Wang
Lei, Weiqiang
Zhou, Taoxun
Qin, Peixi
Zhang, Biying
Hu, Min
author_facet Zhou, Huan
Yuan, Wang
Lei, Weiqiang
Zhou, Taoxun
Qin, Peixi
Zhang, Biying
Hu, Min
author_sort Zhou, Huan
collection PubMed
description BACKGROUND: Ribosome biogenesis is the process of assembling ribosome complexes that regulate cell proliferation and differentiation with potential regulatory effects on development. Many factors regulate ribosome biological processes. Nin one binding protein (Nob1) has received widespread attention as key genes regulating ribosome biogenesis—the 3ʹ end of the 20S rRNA is cleaved by Nob1 at cleavage site D to form 18S rRNA, generating translationally capable 40S subunit. As a ribosome biogenesis factor, Nob1 may regulate the development of organisms, but almost nothing is known about the function of Nob1 for any parasitic nematode. We explored the functional role of NOBP-1 (the homologous gene of Nob1) encoding gene from a parasitic nematode—Strongyloides stercoralis. METHODS: The full-length cDNA, gDNA and promoter region of Ss-nobp-1 was identified using protein BLAST in WormBase ParaSite according to the Caenorhabditis elegans NOBP-1 sequence to analyze the gene structure. RNA sequencing (RNA-seq) data in wormbase were retrieved and analyzed to assess the transcript abundance of Ss-nobp-1 in seven developmental stages of S. stercoralis. The standard method for gonadal microinjection of constructs was carried out to determine the anatomic expression patterns of Ss-nobp-1. The interaction between Ss-NOBP-1 and partner of NOBP-1 (Ss-PNO-1) was assessed by yeast two-hybridization and bimolecular fluorescence complementarity (BiFC) experiments. RESULTS: The NOBP-1 encoding gene Ss-nopb-1 from the zoonotic parasite S. stercoralis has been isolated and characterized. The genomic DNA representing Ss-nobp-1 includes a 1599-bp coding region and encodes a protein comprising 403 amino acids (aa), which contains conserved PIN domain and zinc ribbon domain. RNA-seq analysis revealed that Ss-nobp-1 transcripts are present throughout the seven developmental stages in S. stercoralis and have higher transcription levels in iL3, L3 and P Female. Ss-nobp-1 is expressed mainly in the intestine of transgenic S. stercoralis larvae, and there is a direct interaction between Ss-NOBP-1 and Ss-PNO-1. CONCLUSIONS: Collectively, Ss-NOBP-1 has a potential role in embryo formation and the infective process, and findings from this study provide a sound foundation for investigating its function during the development of parasitic nematode. GRAPHICAL ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13071-023-05940-9.
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spelling pubmed-106238432023-11-04 Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis Zhou, Huan Yuan, Wang Lei, Weiqiang Zhou, Taoxun Qin, Peixi Zhang, Biying Hu, Min Parasit Vectors Research BACKGROUND: Ribosome biogenesis is the process of assembling ribosome complexes that regulate cell proliferation and differentiation with potential regulatory effects on development. Many factors regulate ribosome biological processes. Nin one binding protein (Nob1) has received widespread attention as key genes regulating ribosome biogenesis—the 3ʹ end of the 20S rRNA is cleaved by Nob1 at cleavage site D to form 18S rRNA, generating translationally capable 40S subunit. As a ribosome biogenesis factor, Nob1 may regulate the development of organisms, but almost nothing is known about the function of Nob1 for any parasitic nematode. We explored the functional role of NOBP-1 (the homologous gene of Nob1) encoding gene from a parasitic nematode—Strongyloides stercoralis. METHODS: The full-length cDNA, gDNA and promoter region of Ss-nobp-1 was identified using protein BLAST in WormBase ParaSite according to the Caenorhabditis elegans NOBP-1 sequence to analyze the gene structure. RNA sequencing (RNA-seq) data in wormbase were retrieved and analyzed to assess the transcript abundance of Ss-nobp-1 in seven developmental stages of S. stercoralis. The standard method for gonadal microinjection of constructs was carried out to determine the anatomic expression patterns of Ss-nobp-1. The interaction between Ss-NOBP-1 and partner of NOBP-1 (Ss-PNO-1) was assessed by yeast two-hybridization and bimolecular fluorescence complementarity (BiFC) experiments. RESULTS: The NOBP-1 encoding gene Ss-nopb-1 from the zoonotic parasite S. stercoralis has been isolated and characterized. The genomic DNA representing Ss-nobp-1 includes a 1599-bp coding region and encodes a protein comprising 403 amino acids (aa), which contains conserved PIN domain and zinc ribbon domain. RNA-seq analysis revealed that Ss-nobp-1 transcripts are present throughout the seven developmental stages in S. stercoralis and have higher transcription levels in iL3, L3 and P Female. Ss-nobp-1 is expressed mainly in the intestine of transgenic S. stercoralis larvae, and there is a direct interaction between Ss-NOBP-1 and Ss-PNO-1. CONCLUSIONS: Collectively, Ss-NOBP-1 has a potential role in embryo formation and the infective process, and findings from this study provide a sound foundation for investigating its function during the development of parasitic nematode. GRAPHICAL ABSTRACT: [Image: see text] SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s13071-023-05940-9. BioMed Central 2023-11-03 /pmc/articles/PMC10623843/ /pubmed/37924155 http://dx.doi.org/10.1186/s13071-023-05940-9 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Zhou, Huan
Yuan, Wang
Lei, Weiqiang
Zhou, Taoxun
Qin, Peixi
Zhang, Biying
Hu, Min
Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title_full Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title_fullStr Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title_full_unstemmed Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title_short Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis
title_sort domain definition and preliminary functional exploration of the endonuclease nobp-1 in strongyloides stercoralis
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10623843/
https://www.ncbi.nlm.nih.gov/pubmed/37924155
http://dx.doi.org/10.1186/s13071-023-05940-9
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