The Conserved Family of the Pyridoxal Phosphate-Binding Protein (PLPBP) and Its Cyanobacterial Paradigm PipY
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Título: | The Conserved Family of the Pyridoxal Phosphate-Binding Protein (PLPBP) and Its Cyanobacterial Paradigm PipY |
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Autor/es: | Tremiño, Lorena | Llop Estevez, Antonio | Rubio, Vicente | Contreras, Asunción |
Grupo/s de investigación o GITE: | Transducción de Señales en Bacterias |
Centro, Departamento o Servicio: | Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología |
Palabras clave: | Cyanobacteria | Nitrogen regulation | COG0325 | PLPHP | PLPBP | PipY | YggS | Pyridoxal phosphate | Synechococcus elongatus PCC7942 | Vitamin B6-dependent epilepsy |
Fecha de publicación: | 17-oct-2022 |
Editor: | MDPI |
Cita bibliográfica: | Tremiño L, Llop A, Rubio V, Contreras A. The Conserved Family of the Pyridoxal Phosphate-Binding Protein (PLPBP) and Its Cyanobacterial Paradigm PipY. Life. 2022; 12(10):1622. https://doi.org/10.3390/life12101622 |
Resumen: | The PLPBP family of pyridoxal phosphate-binding proteins has a high degree of sequence conservation and is represented in all three domains of life. PLPBP members, of which a few representatives have been studied in different contexts, are single-domain proteins with no known enzymatic activity that exhibit the fold type III of PLP-holoenzymes, consisting in an α/β barrel (TIM-barrel), where the PLP cofactor is solvent-exposed. Despite the constant presence of cofactor PLP (a key catalytic element in PLP enzymes), PLPBP family members appear to have purely regulatory functions affecting the homeostasis of vitamin B6 vitamers and amino/keto acids. Perturbation of these metabolites and pleiotropic phenotypes have been reported in bacteria and zebrafish after PLPBP gene inactivation as well as in patients with vitamin B6-dependent epilepsy that results from loss-of-function mutations at the PLPBP. Here, we review information gathered from diverse studies and biological systems, emphasizing the structural and functional conservation of the PLPBP members and discussing the informative nature of model systems and experimental approaches. In this context, the relatively high level of structural and functional characterization of PipY from Synechococcus elongatus PCC 7942 provides a unique opportunity to investigate the PLPBP roles in the context of a signaling pathway conserved in cyanobacteria. |
Patrocinador/es: | Work in our laboratories were supported by grants PID220‐118816GB‐I00 and BFU2015‐66360‐P from the Spanish Government (MICINN), grants GRE20‐04‐C, VIGROB20‐126, UADIF20‐34 and UADIF19‐36 from the University of Alicante (to AC) and grant CIVP‐20A6610 from the Fundación Ramón Areces (to VR). |
URI: | http://hdl.handle.net/10045/128660 |
ISSN: | 2075-1729 |
DOI: | 10.3390/life12101622 |
Idioma: | eng |
Tipo: | info:eu-repo/semantics/article |
Derechos: | © 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
Revisión científica: | si |
Versión del editor: | https://doi.org/10.3390/life12101622 |
Aparece en las colecciones: | INV - TSB - Artículos de Revistas |
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