Amb motiu del tancament d'estiu, la validació de documents es reprendrà a partir del 28 d'agost de 2026. Disculpeu les molèsties.
Con motivo del cierre de verano, la validación de documentos se reanudará a partir del 28 de agosto de 2026. Disculpad las molestias
Due to the summer closure, document validation will resume starting August 28, 2026. We apologize for any inconvenience.

Files

621956.pdf (252.83 KB)

Document type

Article

Version

Accepted version

Publication date

2013-02-01

All rights reserved

Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/43402

Protein interaction studies point to new functions for Escherichia coli glyceraldehyde-3-phosphate dehydrogenase

Journal Title

Authors

Director/Tutor

Journal ISSN

Volume Title

Related resource

http://dx.doi.org/10.1016/j.resmic.2012.11.002

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is considered a multifunctional protein with defined functions in numerous mammalian cellular processes. GAPDH functional diversity depends on various factors such as covalent modifications, subcellular localization, oligomeric state and intracellular concentration of substrates or ligands, as well as protein-protein interactions. In bacteria, alternative GAPDH functions have been associated with its extracellular location in pathogens or probiotics. In this study, new intracellular functions of E. coli GAPDH were investigated following a proteomic approach aimed at identifying interacting partners using in vivo formaldehyde cross-linking followed by mass spectrometry. The identified proteins were involved in metabolic processes, protein synthesis and folding or DNA repair. Some interacting proteins were also identified in immunopurification experiments in the absence of cross-linking. Pull-down experiments and overlay immunoblotting were performed to further characterize the interaction with phosphoglycolate phosphatase (Gph). This enzyme is involved in the metabolism of 2-phosphoglycolate formed in the DNA repair of 3"-phosphoglycolate ends generated by bleomycin damage. We show that interaction between Gph and GAPDH increases in cells challenged with bleomycin, suggesting involvement of GAPDH in cellular processes linked to DNA repair mechanisms.

Subject

Proteïnes, Escheríchia coli, Reparació de l'ADN

Subject (English)

Proteins, Escherichia coli, DNA repair

Citation

Collections

Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

Citation

FERREIRA, Elaine, et al. Protein interaction studies point to new functions for Escherichia coli glyceraldehyde-3-phosphate dehydrogenase. Research in Microbiology. 2013. Vol. 164, num. 145-154. ISSN 0923-2508. [consulted: 12 of August of 2026]. Available at: https://hdl.handle.net/2445/43402

Export metadata

JSON - METS

Share record