Role of the N‐terminal signal peptide in the membrane insertion of Aquifex aeolicus F₁F₀ATP synthase c‐subunit

Abstract

Rotary ATPases are membrane protein complexes that couple ATP hydrolysis to ion translocation across the membrane. Overall, they are evolutionarily well conserved, but the N‐terminal segments of their rotary subunits (c‐subunits) possess different lengths and levels of hydrophobicity across species. By analyzing the N‐terminal variability, we distinguish four phylogenetic groups of c‐subunits (groups 1–4). We characterize a member of group 2, the c‐subunit from Aquifex aeolicus F1F0 ATP synthase, both in native cells and in a heterologous expression system. We demonstrate that its N‐terminal segment forms a signal peptide with signal recognition particle (SRP) recognition features and is obligatorily required for membrane insertion. Based on our study and on previous characterizations of c‐subunits from other organisms, we propose that c‐subunits follow different membrane insertion pathways.

Bridged Hybrid Monolithic Column Coupled to High-Resolution Mass Spectrometry for Top-Down Proteomics

“…Importantly, an 88-amino acid removal was characterized at the N-terminus based on the b ions detected, which is not present in the database. The 88-amino acid sequence is likely an N-terminal signal peptide that may play a role in the transportation of ATP synthase into mitochondria and is cleaved off after the transportation . The successful identification of this 51.7 kDa protein with N-terminal amino acid removal also shows the strength of this top-down proteomics platform by combining C8@BTSEY-based RPC with MS analysis.…”

Immunoinformatics and analysis of antigen distribution of Ureaplasma diversum strains isolated from different Brazilian states

“…Rapid analysis of all or part of the genome allows the construction of primers and screening of genes coding for virulence factors in the most diverse bacterial strains. The use of immunoinformatics tools allows screening with a high level of reliability of the physico-chemical and immunological properties of these molecules with low cost and reliable results [9]. The use of recombinant DNA technology can, through expression in a heterologous system, allow the analysis of virulence factors alone.…”

Evaluation of Different Signal Peptides for Secretory Production of Recombinant Bovine Pancreatic Ribonuclease A in Gram Negative Bacterial System: An In silico Study

“…N and h-regions have vital role in transferring proteins to periplasmic space [16][17][18], whereas c-region plays a key role as a cleavable site which can be recognized by signal peptidase. Despite SPs important role in the production of recombinant protein, there has been no universal approach to detect them [16,19]. In recent decades with the increase in biological data, biologists are mostly applying intelligence method such as machine learning to analyze the data [20], as in today, in silico analysis and bioinformatics tools have attracted special attention in biology, because they not only decrease the high cost of experiments but also provide reliable results [17].…”