Genomic Analysis of Intrinsically Disordered Proteins in the Genus Camelus

Abstract

Intrinsically disordered proteins/regions (IDPs/IDRs) fail to fold completely into 3D structures, but have major roles in determining protein function. While natively disordered proteins/regions have been found to fulfill a wide variety of primary cellular roles, the functions of many disordered proteins in numerous species remain to be uncovered. Here, we perform the first large-scale study of IDPs/IDRs in the genus Camelus, one of the most important mammalians in Asia and North Africa, in order to explore the biological roles of these proteins. The study includes the prediction of disordered proteins/regions in Camelus species and in humans using multiple state-of-the-art prediction tools. Additionally, we provide a comparative analysis of Camelus and Homo sapiens IDPs/IDRs for the sake of highlighting the distinctive use of disorder in each genus. Our findings indicate that the human proteome is more disordered than the Camelus proteome. Gene Ontology analysis also revealed that Camelus IDPs are enriched in glutathione catabolism and lactose biosynthesis.

Comparative analysis of transposable elements provides insights into genome evolution in the genus Camelus

“…Camels can fluctuate their body temperature from 34 ∘ C to 41.7 ∘ C and can conserve water by not sweating [ 2 ]. Additional members of the camelid family included in our study are the Bactrian camel ( Camelus bactrianus ) and the Wild Bactrian camel ( Camelus ferus ) of Asia, and the alpaca ( Vicugna pacos ) of South America [ 4 , 38 ]. The extreme variation among their natural habitats opens up a series of questions about how the environment influences TEs in camelids.…”

A previously-unrecognized motif of transcription factor RYBP, hotspot of cancer-related mutations, is essential for the integrity ofPolycombrepressive complex 1

“…upon PRC1 trimer formation, as recently demonstrated for other similar motifs (Alderson et al, 2023). Considering that about 34% of the human proteome codes for intrinsically disordered regions, with ∼47% of proteins containing long disordered regions (≥30 disordered residues, with an average length of 214 residues, (Alshehri et al, 2020)), our study shows how important it is to systematically characterize those regions computationally and experimentally.…”

On the Prevalence and Potential Functionality of an Intrinsic Disorder in the MERS-CoV Proteome

“…The function of a given protein is often determined by its 3D structure; however, comparative studies on structure-to-function mechanisms have led to the realization that some proteins lack stable 3D structures in whole or in part, yet still play critical functions in the cell. Such proteins/regions with no well-defined stable structure are known as intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs), and occur throughout eukaryotic proteomes [ 9 , 10 , 11 ]. Disordered segments of at least 30 consecutive residues in length are termed long disordered regions (LDRs), and have been previously used as markers to distinguish disordered proteins [ 12 ].…”

“…In particular, conformational flexibility allows disordered proteins to interact with multiple partners using a larger interaction surface, which translates into greater versatility and speed of interaction. It has been shown that protein disorder is significantly involved in molecular recognition processes, intracellular signalling machinery, and post-translational modifications [ 11 , 13 ]; disordered proteins thus contribute to the regulation of various biological processes [ 14 , 15 ]. Furthermore, although IDPs/IDRs are widespread in eukaryotic proteomes, relative to the three domains of life (archaea, bacteria, and eukaryotes), viruses are characterized by the widest spread of disordered proteome content [ 16 ].…”