Theoretical ribosomal protein mass distribution of Pseudomonas aeruginosa PAO1
- Published
- Accepted
- Subject Areas
- Biochemistry, Bioengineering, Bioinformatics, Biotechnology, Microbiology
- Keywords
- large subunit, ribosomal proteins, small subunit, mass spectrometry, MALDI-TOF MS, ribosome, mass resolution
- Copyright
- © 2018 Ng
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
- Cite this article
- 2018. Theoretical ribosomal protein mass distribution of Pseudomonas aeruginosa PAO1. PeerJ Preprints 6:e3500v1 https://doi.org/10.7287/peerj.preprints.3500v1
Abstract
Ribosomes are the protein synthesis factories of a cell and thus are evolutionary conserved in structure and function. Comprising a large and small subunit, the ribosome is further made up of ribosomal proteins that give structure and function to different parts of the macromolecular complex. Current methods for isolating the ribosome include density gradient ultracentrifugation that separates the ribosome into the large and small subunit. Separation of the various ribosomal proteins that comprise each of the subunit would require a solubilization step followed by the use of sodium dodecyl sulphate and polyacrylamide gel electrophoresis (SDS-PAGE). However, possibility exists for the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the set of ribosomal proteins that could be solubilized from each ribosome subunit. Using ribosomal protein amino acid sequence information from Kyoto Encyclopaedia of Genes and Genomes (KEGG), the molecular weight of each ribosomal protein from Pseudomonas aeruginosa PAO1 was calculated in this report. Obtained results revealed that each ribosomal protein had a unique mass that could be detected by mid-range MALDI-TOF MS instruments. More importantly, the mass of ribosomal proteins constitutes a unique mass fingerprint of each ribosome subunit, which accounts for the different structure and functions of the large and small ribosome subunit. Overall, current mass resolution of MALDI-TOF MS instruments could resolve ribosomal proteins and thus provides a tool for profiling the set of ribosomal proteins that constitute the large and small subunit of the ribosome.
Author Comment
This is a preprint manuscript.
Supplemental Information
Theoretical molecular mass of ribosomal proteins of Pseudomonas aeruginosa PAO1
Molecular mass of ribosomal proteins of the large and small ribosome subunit of Pseudomonas aeruginosa PAO1