Investigating Camel Superoxide Dismutase 1: A Computational Analysis of Potential Key Player in Heat Stress Adaptation

Background. Superoxide dismutase 1 (SOD1) is crucial for cellular defense against oxidative stress induced by superoxide radicals, particularly in challenging conditions, such as elevated temperature and humidity. This study investigated SOD1 in Bactrian camel (Camelus bactrianus), Wild Bactrian camel (C. ferus), and Arabian camel (C. dromedarius) to understand its role in heat tolerance. Methodology. The current study employed bioinformatics analysis to assess the genomic features including GC% content. It also investigated the structure and location of the SOD1 gene on the chromosomes. Phylogenetic analysis was conducted to elucidate the evolutionary relationships based on SOD1 protein sequences. Structural analyses encompassed secondary and tertiary structure predictions, emphasizing stability and potential functional implications. Subcellular localization of the SOD1 protein was also explored. Results. C. dromedarius displayed the highest GC% in its genome, indicating improved thermostability. With the exception of C. bactrianus whose chromosomal location was unknown, all other species contained SOD1 gene on their first chromosome. Based upon SOD1 protein sequences, phylogenetic investigation emphasized the close evolutionary link within the Camelidae family. Structurally, all three species of camel shared an acidic, globular, and thermally-stable SOD1 protein having high glycine content and lack of cleavage sites. Analysis of secondary structure indicated a frequency of random coils, highlighting the adaptability and evolutionary conservation of protein. Predictions of tertiary structure verified that SOD1 was stable in all species. The protein is predominantly found in cytoplasm although, also present in nucleus, extracellular region, and mitochondria. Conclusion. This inclusive analysis of SOD1 in three different species of camel highlighted their strong adaptation to desert environment by elucidating their genomic and proteomic stability. Further research is necessary to investigate the biochemical mechanisms behind camels’ extraordinary ability to thrive in desert conditions and respond to the challenges posed by climate change.

Authors

Institutions

Publication Details

Journal
BioScientific Review
Published
2025-05-02
DOI
https://doi.org/10.32350/bsr.71.07
Primary Topic
Heat shock proteins research
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Investigating Camel Superoxide Dismutase 1: A Computational Analysis of Potential Key Player in Heat Stress Adaptation

M. A. Khan, Muhammad Abrar Yousaf
BioScientific Review
Heat shock proteins research
article

Investigating Camel Superoxide Dismutase 1: A Computational Analysis of Potential Key Player in Heat Stress Adaptation

M. A. Khan, Muhammad Abrar Yousaf
article en

Abstract

Background. Superoxide dismutase 1 (SOD1) is crucial for cellular defense against oxidative stress induced by superoxide radicals, particularly in challenging conditions, such as elevated temperature and humidity. This study investigated SOD1 in Bactrian camel (Camelus bactrianus), Wild Bactrian camel (C. ferus), and Arabian camel (C. dromedarius) to understand its role in heat tolerance. Methodology. The current study employed bioinformatics analysis to assess the genomic features including GC% content. It also investigated the structure and location of the SOD1 gene on the chromosomes. Phylogenetic analysis was conducted to elucidate the evolutionary relationships based on SOD1 protein sequences. Structural analyses encompassed secondary and tertiary structure predictions, emphasizing stability and potential functional implications. Subcellular localization of the SOD1 protein was also explored. Results. C. dromedarius displayed the highest GC% in its genome, indicating improved thermostability. With the exception of C. bactrianus whose chromosomal location was unknown, all other species contained SOD1 gene on their first chromosome. Based upon SOD1 protein sequences, phylogenetic investigation emphasized the close evolutionary link within the Camelidae family. Structurally, all three species of camel shared an acidic, globular, and thermally-stable SOD1 protein having high glycine content and lack of cleavage sites. Analysis of secondary structure indicated a frequency of random coils, highlighting the adaptability and evolutionary conservation of protein. Predictions of tertiary structure verified that SOD1 was stable in all species. The protein is predominantly found in cytoplasm although, also present in nucleus, extracellular region, and mitochondria. Conclusion. This inclusive analysis of SOD1 in three different species of camel highlighted their strong adaptation to desert environment by elucidating their genomic and proteomic stability. Further research is necessary to investigate the biochemical mechanisms behind camels’ extraordinary ability to thrive in desert conditions and respond to the challenges posed by climate change.

BioScientific ReviewVol. 7(1)
University of Verona (IT), Virtual University of Pakistan (PK)
Openalex Percentile: Top 90%
Heat shock proteins research
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.