Identification, Genomic Characterization, and Phylogenetic Relationship of the Heat Shock Protein Beta-1 (HSPB1) in Placental Mammals

Heat Shock Protein Beta-1 (HSPB1), a molecular chaperone crucial for cellular response and proteostasis, exhibits evolutionary conservation with potential lineage-specific adaptations in placental mammals, warranting detailed comparative genomic investigation. The study investigated the characteristics, evolutionary links, motifs, secondary structure, and genetic organization of the HSPB1 protein across twelve distinct mammals. Significant sequence conservation was identified using multiple sequence alignments (MSA), with over 70% identity in specific areas among the represented species. Physiochemical analysis revealed that all species’ protein sequences exhibited an acidic nature, while instability indices indicated inherent protein instability. The GRAVY analysis referred to hydrophilic properties, while the aliphatic index showed heat stability. Phylogenetic analysis revealed five distinct clades, corresponding to major placental mammals groups (e.g. Homo sapiens, Bos Taurus), which underscores deep evolutionary divergences and conserved stress-response adaptations across lineages. Motif analysis revealed distinctive patterns in several species, and InterProScan results revealed membership in the "Homologous superfamily HSP20_like_Chapserson" family. An examination of the genetic organization indicated differences among all the represented species in the upstream, downstream, intron, and CDS regions, and the presence of conserved regions suggested their identity and similarity matrices. The current study conducted a computational approach and supporting evidence that HSPB1 is a novel heat shock responsive protein identified in placental mammals. The current study findings provide a foundational framework delving into HSPB1 evolutionary and lineage-specific diversification, offering valuable insights into stress adaptation mechanisms and their implications for biomedical or evolutionary studies in mammals.

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Publication Details

Journal
Journal of Zoology and Systematics
Published
2025-04-12
DOI
https://doi.org/10.56946/jzs.v3i1.546
Citations
1
Primary Topic
Heat shock proteins research
Type
article
Field-Weighted Citation Impact
0.81
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article

Identification, Genomic Characterization, and Phylogenetic Relationship of the Heat Shock Protein Beta-1 (HSPB1) in Placental Mammals

Muhammad Farhan Khan, Shakeela Parveen, Sarwar Jahan, Muhammad Azhar Hussain et al.
1 citations
Journal of Zoology and Systematics
Heat shock proteins research
0.81
article

Identification, Genomic Characterization, and Phylogenetic Relationship of the Heat Shock Protein Beta-1 (HSPB1) in Placental Mammals

Muhammad Farhan Khan, Shakeela Parveen, Sarwar Jahan, Muhammad Azhar Hussain, Ayesha Khan, Muhammad Tayyab, Mehwish Sultana, Muhammad Abdul Manan
article en
1 citations

Abstract

Heat Shock Protein Beta-1 (HSPB1), a molecular chaperone crucial for cellular response and proteostasis, exhibits evolutionary conservation with potential lineage-specific adaptations in placental mammals, warranting detailed comparative genomic investigation. The study investigated the characteristics, evolutionary links, motifs, secondary structure, and genetic organization of the HSPB1 protein across twelve distinct mammals. Significant sequence conservation was identified using multiple sequence alignments (MSA), with over 70% identity in specific areas among the represented species. Physiochemical analysis revealed that all species’ protein sequences exhibited an acidic nature, while instability indices indicated inherent protein instability. The GRAVY analysis referred to hydrophilic properties, while the aliphatic index showed heat stability. Phylogenetic analysis revealed five distinct clades, corresponding to major placental mammals groups (e.g. Homo sapiens, Bos Taurus), which underscores deep evolutionary divergences and conserved stress-response adaptations across lineages. Motif analysis revealed distinctive patterns in several species, and InterProScan results revealed membership in the "Homologous superfamily HSP20_like_Chapserson" family. An examination of the genetic organization indicated differences among all the represented species in the upstream, downstream, intron, and CDS regions, and the presence of conserved regions suggested their identity and similarity matrices. The current study conducted a computational approach and supporting evidence that HSPB1 is a novel heat shock responsive protein identified in placental mammals. The current study findings provide a foundational framework delving into HSPB1 evolutionary and lineage-specific diversification, offering valuable insights into stress adaptation mechanisms and their implications for biomedical or evolutionary studies in mammals.

Journal of Zoology and Systematics
Gomal University (PK), University of the Punjab (PK), Government College University, Faisalabad (PK), Government Sadiq College Women University (PK), Government of Khyber Pakhtunkhwa (PK), University of Veterinary and Animal Sciences (PK)
Openalex Percentile: Top 29%
Heat shock proteins research
0.81
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