TAILIEUCHUNG - Báo cáo khoa học: Functional analysis of two divalent metal-dependent regulatory genes dmdR1 and dmdR2 in Streptomyces coelicolor and proteome changes in deletion mutants

In Gram-positive bacteria, the expression of iron-regulated genes is medi-ated by a class of divalent metal-dependent regulatory (DmdR) proteins. We cloned and characterized twodmdR genes of Streptomyces coelicolor that were located in two different nonoverlapping cosmids. Functional ana-lysis of dmdR1anddmdR2was performed by deletion of each copy. Dele-tion of dmdR1resulted in the derepression of at least eight proteins and in the repression of three others, as shown by 2D proteome analysis. | ềFEBS Journal Functional analysis of two divalent metal-dependent regulatory genes dmdRI and dmdR2 in Streptomyces coelicolor and proteome changes in deletion mutants Francisco J. Flores1 Carlos Barreiro2 Juan Jose R. Coque1 2 and Juan F. Martin1 2 1 Area de Microbiologia Facultad de Ciencias Biologicas y Ambientales Universidad de Leon Spain 2 Institute of Biotechnology of Leon INBIOTEC Parque Cientifico de Leon Spain Keywords iron metabolism proteome changes regulatory proteins Streptomyces Correspondence J. F. Martin Area de Microbiologia Facultad de Ciencias Biologicas y Ambientales Universidad de Leon 24071 Leon Spain Fax 34 987 291506 Tel 34 987 291505 E-mail degjmm@ Received 13 September 2004 revised 11 November 2004 accepted 29 November 2004 doi In Gram-positive bacteria the expression of iron-regulated genes is mediated by a class of divalent metal-dependent regulatory DmdR proteins. We cloned and characterized two dmdR genes of Streptomyces coelicolor that were located in two different nonoverlapping cosmids. Functional analysis of dmdRl and dmdR2 was performed by deletion of each copy. Deletion of dmdRl resulted in the derepression of at least eight proteins and in the repression of three others as shown by 2D proteome analysis. These 11 proteins were characterized by MALDI-TOF peptide mass fingerprinting. The proteins that show an increased level in the mutant correspond to a DNA-binding hemoprotein iron-metabolism proteins and several divalent metal-regulated enzymes. The levels of two other proteins - a superoxide dismutase and a specific glutamatic dehydrogenase - were found to decrease in this mutant. Complementation of the dmdRl-deletion mutant with the wild-type dmdRl allele restored the normal proteome profile. By contrast deletion of dmdR2 did not affect significantly the protein profile of S. coelicolor. One of the proteins P1 a phosphatidylethanolamine-binding protein overexpressed in the .

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