Shot-gun proteomics: why thousands of unidentified signals matter. Issue 1 (20th December 2019)
- Record Type:
- Journal Article
- Title:
- Shot-gun proteomics: why thousands of unidentified signals matter. Issue 1 (20th December 2019)
- Main Title:
- Shot-gun proteomics: why thousands of unidentified signals matter
- Authors:
- den Ridder, Maxime
Daran-Lapujade, Pascale
Pabst, Martin - Abstract:
- ABSTRACT: Mass spectrometry-based proteomics has become a constitutional part of the multi-omics toolbox in yeast research, advancing fundamental knowledge of molecular processes and guiding decisions in strain and product developmental pipelines. Nevertheless, post-translational protein modifications (PTMs) continue to challenge the field of proteomics. PTMs are not directly encoded in the genome; therefore, they require a sensitive analysis of the proteome itself. In yeast, the relevance of post-translational regulators has already been established, such as for phosphorylation, which can directly affect the reaction rates of metabolic enzymes. Whereas, the selective analysis of single modifications has become a broadly employed technique, the sensitive analysis of a comprehensive set of modifications still remains a challenge. At the same time, a large number of fragmentation spectra in a typical shot-gun proteomics experiment remain unidentified. It has been estimated that a good proportion of those unidentified spectra originates from unexpected modifications or natural peptide variants. In this review, recent advancements in microbial proteomics for unrestricted protein modification discovery are reviewed, and recent research integrating this additional layer of information to elucidate protein interaction and regulation in yeast is briefly discussed. Abstract : The authors review recent developments in yeast proteomics for the discovery and analysis ofABSTRACT: Mass spectrometry-based proteomics has become a constitutional part of the multi-omics toolbox in yeast research, advancing fundamental knowledge of molecular processes and guiding decisions in strain and product developmental pipelines. Nevertheless, post-translational protein modifications (PTMs) continue to challenge the field of proteomics. PTMs are not directly encoded in the genome; therefore, they require a sensitive analysis of the proteome itself. In yeast, the relevance of post-translational regulators has already been established, such as for phosphorylation, which can directly affect the reaction rates of metabolic enzymes. Whereas, the selective analysis of single modifications has become a broadly employed technique, the sensitive analysis of a comprehensive set of modifications still remains a challenge. At the same time, a large number of fragmentation spectra in a typical shot-gun proteomics experiment remain unidentified. It has been estimated that a good proportion of those unidentified spectra originates from unexpected modifications or natural peptide variants. In this review, recent advancements in microbial proteomics for unrestricted protein modification discovery are reviewed, and recent research integrating this additional layer of information to elucidate protein interaction and regulation in yeast is briefly discussed. Abstract : The authors review recent developments in yeast proteomics for the discovery and analysis of post-translational modifications, which are important regulators in many cellular processes of yeast. … (more)
- Is Part Of:
- FEMS yeast research. Volume 20:Issue 1(2020)
- Journal:
- FEMS yeast research
- Issue:
- Volume 20:Issue 1(2020)
- Issue Display:
- Volume 20, Issue 1 (2020)
- Year:
- 2020
- Volume:
- 20
- Issue:
- 1
- Issue Sort Value:
- 2020-0020-0001-0000
- Page Start:
- Page End:
- Publication Date:
- 2019-12-20
- Subjects:
- Mass spectrometry -- post-translational modifications -- unrestricted modification search -- protein regulation -- yeast proteomics
Yeast -- Periodicals
Yeasts -- Periodicals
579.562 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1567-1364 ↗
http://www.sciencedirect.com/science/journal/15671356 ↗
http://www.blackwell-synergy.com/rd.asp?goto=journal&code=fyr ↗
http://onlinelibrary.wiley.com/ ↗
http://femsyr.oxfordjournals.org/content/ ↗ - DOI:
- 10.1093/femsyr/foz088 ↗
- Languages:
- English
- ISSNs:
- 1567-1356
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.325000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23382.xml