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dc.contributor.author
Sastre, Diego Emiliano  
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Pulschen, André A.  
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Basso, Luis G.M.  
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Benites Pariente, Jhonathan S.  
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Marques Netto, Caterina G.C.  
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Machinandiarena, Federico  
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Albanesi, Daniela  
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Navarro, Marcos V.A.S.  
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de Mendoza, Diego  
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Gueiros Filho, Frederico J.  
dc.date.available
2023-01-27T18:20:03Z  
dc.date.issued
2020-02  
dc.identifier.citation
Sastre, Diego Emiliano; Pulschen, André A.; Basso, Luis G.M.; Benites Pariente, Jhonathan S.; Marques Netto, Caterina G.C.; et al.; The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis; Elsevier; Journal of Biological Chemistry (online); 295; 7; 2-2020; 2148-2159  
dc.identifier.issn
0021-9258  
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http://hdl.handle.net/11336/185996  
dc.description.abstract
PlsX is the first enzyme in the pathway that produces phosphatidic acid in Gram-positive bacteria. It makes acylphosphate from acyl-acyl carrier protein (acyl-ACP) and is also involved in coordinating phospholipid and fatty acid biosyntheses. PlsX is a peripheral membrane enzyme in Bacillus subtilis, but how it associates with the membrane remains largely unknown. In the present study, using fluorescence microscopy, liposome sedimentation, differential scanning calorimetry, and acyltransferase assays, we determined that PlsX binds directly to lipid bilayers and identified its membrane anchoring moiety, consisting of a hydrophobic loop located at the tip of two amphipathic dimerization helices. To establish the role of the membrane association of PlsX in acylphosphate synthesis and in the flux through the phosphatidic acid pathway, we then created mutations and gene fusions that prevent PlsX's interaction with the membrane. Interestingly, phospholipid synthesis was severely hampered in cells in which PlsX was detached from the membrane, and results from metabolic labeling indicated that these cells accumulated free fatty acids. Because the same mutations did not affect PlsX transacylase activity, we conclude that membrane association is required for the proper delivery of PlsX's product to PlsY, the next enzyme in the phosphatidic acid pathway. We conclude that PlsX plays a dual role in phospholipid synthesis, acting both as a catalyst and as a chaperone protein that mediates substrate channeling into the pathway.  
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application/pdf  
dc.language.iso
eng  
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Elsevier  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/  
dc.subject
GLYCEROPHOSPHOLIPID  
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GRAM-POSITIVE BACTERIA  
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MEMBRANE BIOGENESIS  
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ACYLTRANSFERASE  
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LIPID BINDING PROTEIN  
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PLSX  
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ACYLPHOSPHATE  
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SUBSTRATE CHANNELING  
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PROTEIN-MEMBRANE INTERACTION  
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PHOSPHATIDIC ACID  
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Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
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Biología Celular, Microbiología  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
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Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2021-09-06T21:07:13Z  
dc.identifier.eissn
1083-351X  
dc.journal.volume
295  
dc.journal.number
7  
dc.journal.pagination
2148-2159  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Ámsterdam  
dc.description.fil
Fil: Sastre, Diego Emiliano. Universidade de Sao Paulo; Brasil. Instituto de Química ; Universidade Do Sao Paulo;  
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Fil: Pulschen, André A.. Instituto de Química ; Universidade Do Sao Paulo;  
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Fil: Basso, Luis G.M.. Universidade de Sao Paulo; Brasil  
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Fil: Benites Pariente, Jhonathan S.. Instituto de Química ; Universidade Do Sao Paulo;  
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Fil: Marques Netto, Caterina G.C.. Universidade Federal do São Carlos; Brasil  
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Fil: Machinandiarena, Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina  
dc.description.fil
Fil: Albanesi, Daniela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina  
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Fil: Navarro, Marcos V.A.S.. Universidade de Sao Paulo; Brasil  
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Fil: de Mendoza, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina  
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Fil: Gueiros Filho, Frederico J.. Universidade de Sao Paulo; Brasil  
dc.journal.title
Journal of Biological Chemistry (online)  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.RA119.011147  
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info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021925817482895