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Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo

Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat,...

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Autores principales: Rehman, Muhammad Saif-ur, Hassan, Faiz-ul, Rehman, Zia-ur, Hussain, Hafiz Noubahar, Shahid, Muhammad Adnan, Mushahid, Muhammad, Shokrollahi, Borhan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9553489/
https://www.ncbi.nlm.nih.gov/pubmed/36246983
http://dx.doi.org/10.1155/2022/1581714
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author Rehman, Muhammad Saif-ur
Hassan, Faiz-ul
Rehman, Zia-ur
Hussain, Hafiz Noubahar
Shahid, Muhammad Adnan
Mushahid, Muhammad
Shokrollahi, Borhan
author_facet Rehman, Muhammad Saif-ur
Hassan, Faiz-ul
Rehman, Zia-ur
Hussain, Hafiz Noubahar
Shahid, Muhammad Adnan
Mushahid, Muhammad
Shokrollahi, Borhan
author_sort Rehman, Muhammad Saif-ur
collection PubMed
description Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo.
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spelling pubmed-95534892022-10-13 Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo Rehman, Muhammad Saif-ur Hassan, Faiz-ul Rehman, Zia-ur Hussain, Hafiz Noubahar Shahid, Muhammad Adnan Mushahid, Muhammad Shokrollahi, Borhan Biomed Res Int Research Article Relaxin family peptides significantly regulate reproduction, nutrient metabolism, and immune response in mammals. The present study aimed to identify and characterize the relaxin family peptides in cattle and buffalo at the genome level. The genomic and proteomic sequences of cattle, buffalo, goat, sheep, horse, and camel were accessed through the NCBI database, and BLAST was performed. We identified four relaxin peptides genes (RLN3, INSL3, INSL5, and INSL6) in Bos taurus, whereas three relaxin genes (RLN3, INSL3, and INSL6) in Bubalus bubalis. Evolutionary analysis revealed the conserved nature of relaxin family peptides in buffalo and cattle. Physicochemical properties revealed that relaxin proteins were thermostable, hydrophilic, and basic peptides except for INSL5 which was an acidic peptide. Three nonsynonymous mutations (two in RLN3 at positions A16 > T and P29 > A, and one in INSL6 at position R32 > Q) in Bos taurus, whereas two nonsynonymous mutations (one in RLN3 at positions G105 > w and one in INSL3 at position G22 > R) in Bubalus bubalis, were identified. INSL3 had one indel (insertion) at position 55 in Bos taurus. Gene duplication analysis revealed predominantly segmental duplications (INSL5/RLN3 and INSL6/INSL3 gene pairs) that helped expand this gene family, whereas Bubalus bubalis showed primarily tandem duplication (INSL3/RLN3). Our study concluded that relaxin family peptides remained conserved during the evolution, and gene duplications might help to adapt and enrich specific functions like reproduction, nutrient metabolism, and immune response. Further, the nonsynonymous mutations identified potentially affect these functions in buffalo. Hindawi 2022-10-04 /pmc/articles/PMC9553489/ /pubmed/36246983 http://dx.doi.org/10.1155/2022/1581714 Text en Copyright © 2022 Muhammad Saif-ur Rehman et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Rehman, Muhammad Saif-ur
Hassan, Faiz-ul
Rehman, Zia-ur
Hussain, Hafiz Noubahar
Shahid, Muhammad Adnan
Mushahid, Muhammad
Shokrollahi, Borhan
Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title_full Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title_fullStr Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title_full_unstemmed Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title_short Comparative Genomic Characterization of Relaxin Peptide Family in Cattle and Buffalo
title_sort comparative genomic characterization of relaxin peptide family in cattle and buffalo
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9553489/
https://www.ncbi.nlm.nih.gov/pubmed/36246983
http://dx.doi.org/10.1155/2022/1581714
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