Back to Search Start Over

In-gel protein digestion using acidic methanol produces a highly selective methylation of glutamic acid residues.

Authors :
Lozano-Prieto M
Camafeita E
Jorge I
Laguillo-Gómez A
Barrero-Rodríguez R
Devesa CA
Pertusa C
Calvo E
Sánchez-Madrid F
Vázquez J
Martin-Cofreces NB
Source :
Journal of proteomics [J Proteomics] 2024 Jul 30; Vol. 304, pp. 105229. Date of Electronic Publication: 2024 Jun 14.
Publication Year :
2024

Abstract

Mass-tolerant open search methods allow the high-throughput analysis of modified peptides by mass spectrometry. These techniques have paved the way to unbiased analysis of post-translational modifications in biological contexts, as well as of chemical modifications produced during the manipulation of protein samples. In this work, we have analyzed in-depth a wide variety of samples of different biological origin, including cells, extracellular vesicles, secretomes, centrosomes and tissue preparations, using Comet-ReCom, a recently improved version of the open search engine Comet-PTM. Our results demonstrate that glutamic acid residues undergo intensive methyl esterification when protein digestion is performed using in-gel techniques, but not using gel-free approaches. This effect was highly specific to Glu and was not found for other methylable residues such as Asp.<br />Competing Interests: Declaration of competing interest The authors declare no competing interests.<br /> (Copyright © 2024 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1876-7737
Volume :
304
Database :
MEDLINE
Journal :
Journal of proteomics
Publication Type :
Academic Journal
Accession number :
38880355
Full Text :
https://doi.org/10.1016/j.jprot.2024.105229