Deletion of the hypothetical protein SCO2127 of Streptomyces coelicolor allowed identification of a new regulator of actinorhodin production.
Although the specific function of SCO2127 remains elusive, it has been assumed that this hypothetical protein plays an important role in carbon catabolite regulation and therefore in antibiotic biosynthesis in Streptomyces coelicolor. To shed light on the functional relationship of SCO2127 to the biosynthesis of actinorhodin, a detailed analysis of the proteins differentially produced between the strain M145 and the Δsco2127 mutant of S. coelicolor was performed. The delayed morphological differentiation and impaired production of actinorhodin showed by the deletion strain were accompanied by increased abundance of gluconeogenic enzymes, as well as downregulation of both glycolysis and acetyl-CoA carboxylase. Repression of mycothiol biosynthetic enzymes was further observed in the absence of SCO2127, in addition to upregulation of hydroxyectoine biosynthetic enzymes and SCO0204, which controls nitrite formation. The data generated in this study reveal that the response regulator SCO0204 greatly contributes to prevent the formation of actinorhodin in the ∆sco2127 mutant, likely through the activation of some proteins associated with oxidative stress that include the nitrite producer SCO0216.
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Víctor H
VH
Tierrafría
Australian Institute for Bioengineering and Nanotechnology (AIBN), The University of Queensland, St Lucia, Brisbane, Australia.
Cuauhtemoc
C
Licona-Cassani
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Nidia
N
Maldonado-Carmona
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Alba
A
Romero-Rodríguez
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Sara
S
Centeno-Leija
Australian Institute for Bioengineering and Nanotechnology (AIBN), The University of Queensland, St Lucia, Brisbane, Australia.
Esteban
E
Marcellin
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Romina
R
Rodríguez-Sanoja
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico.
Beatriz
B
Ruiz-Villafán
Laboratorio de Bioingeniería, Universidad de Colima, Coquimatlán-, 28400, Colima, Mexico.
Lars K
LK
Nielsen
Instituto de Investigaciones Biomédicas. 3er Circuito Exterior s/n, Universidad Nacional Autónoma de México (UNAM), 04510, Ciudad de México, Mexico. sersan@biomedicas.unam.mx.
Sergio
S
Sánchez
D000880:Anthraquinones / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics*; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial; D048372:Streptomyces coelicolor / Q000235:genetics* / Q000378:metabolism*; D000095622:Benzoisochromanequinones
D000880:Anthraquinones; D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; C013390:actinorhodin; D000095622:Benzoisochromanequinones
Actinorhodin; Nitrite production; Oxidative stress; Proteome analysis; Regulatory network; Streptomyces coelicolor