Chromosome-Level Genome Assembly of the Cape Cliff Lizard (Hemicordylus capensis)

Abstract

Squamates represent a highly diverse and species-rich vertebrate group that is remarkably understudied from a genomic perspective. A scarcity of genomic data is particularly evident for scincomorph lizards, which encompass over 10% of all living squamates, and for which high-quality genomic resources are currently lacking. To address this knowledge gap, we present the first chromosome-level reference genome for this group, generated from a male Cape cliff lizard (Hemicordylus capensis), using highly accurate PacBio HiFi long-read sequencing data, long-range Omni-C chromosomal conformation capture data and transcriptomic data for annotation. The rHemCap1.1 genome assembly spans 2.29 Gb, with a scaffold N50 of 359.65 Mb, and includes 25,300 protein-coding genes, with a BUSCO completeness score of 95.5% (sauropsida_odb10). We have generated the most contiguous and complete chromosome-level squamate reference genome assembly publicly available to date. Furthermore, we used short-read resequencing of 35 males and females and applied a differential coverage approach to infer the sex-determination system of the species, which was previously unknown. Our results suggest this species has XX/XY sex chromosomes, representing the first evidence of sex determination in the family Cordylidae. This reference genome will help to establish this species as an evolutionary model for studying variation in body armour, a key trait in cordylids and other squamate groups. Lastly, this is the first squamate reference genome from a continental African species and, as such, represents a valuable resource not only for further evolutionary research in cordylids but also in closely related groups.

Identification of a Novel Bioactive Peptide Derived from Frozen Chicken Breast Hydrolysate and the Utilization of Hydrolysates as Biopreservatives

“…The observed molecular weight was almost identical to that calculated from the identified amino acid sequence. A database exploration revealed that C25 had a high similarity to partial sequences of beta-enolase enzymes [ 27 ]. The secondary structure was suggested by using the GOR method, which indicated that C25 potentially forms extended strands and random coils ( Figure 3 ).…”

“…The secondary structure was suggested by using the GOR method, which indicated that C25 potentially forms extended strands and random coils (Figure 3). exploration revealed that C25 had a high similarity to partial sequences of beta-eno enzymes [27]. The secondary structure was suggested by using the GOR method, wh indicated that C25 potentially forms extended strands and random coils (Figure 3).…”

“…Interestingly, the chicken hydrolysate and C25 also sho antibacterial activity toward the multi-drug resistant bacterium Proteus vulgaris F24B. exploration revealed that C25 had a high similarity to partial sequences of beta-enolase enzymes [27]. The secondary structure was suggested by using the GOR method, which indicated that C25 potentially forms extended strands and random coils (Figure 3).…”