TAILIEUCHUNG - Báo cáo khoa học: Fluorescence studies of the replication initiator protein RepA in complex with operator and iteron sequences and free in solution

RepA, the replication initiator protein from thePseudomonasplasmid pPS10, regulates plasmid replication and copy number. It is capable of autorepression, in which case it binds as a dimer to the inverted repeat oper-ator sequence preceding its own gene. | ỊFEBS Journal Fluorescence studies of the replication initiator protein RepA in complex with operator and iteron sequences and free in solution Rutger E. M. Diederix1 2 Cristina Davila1 2 Rafael Giraldo2 and M. Pilar Lillo1 1 Departamento de Biofisica Institute de Quimica Fisica Rocasolano CSIC Madrid Spain 2 Departamento de Microbiologia Molecular Centro de Investigaciones Biologicas CSIC Madrid Spain Keywords anisotropy DNA replication fluorescence hydrodynamics RepA Correspondence M. P. Lillo Departamento de Biofisica Instituto de Quimica Fisica Rocasolano CSIC Serrano 119 28006 Madrid Spain Fax 34 91 564 2431 Tel 34 91 561 9400 ext. 1027 E-mail Received 26 June 2008 revised 8 August 2008 acccepted 5 September 2008 doi RepA the replication initiator protein from the Pseudomonas plasmid pPS10 regulates plasmid replication and copy number. It is capable of autorepression in which case it binds as a dimer to the inverted repeat operator sequence preceding its own gene. RepA initiates plasmid replication by binding as a monomer to a series of four adjacent iterons which contain the same half-repeat as found in the operator sequence. RepA contains two domains one of which binds specifically to the half-repeat. The other is the dimerization domain which is involved in protein-protein interactions in the dimeric RepA-operon complex but which actually binds DNA in the monomeric RepA-iteron complex. Here detailed fluorescence studies on RepA and an N- iodoacetyl aminoethyl-8-naphthylamine-1-sulfonic acid-labeled single-cysteine mutant of RepA Cys160 are described. Using time-resolved fluorescence depolarization measurements the global rotational correlation times of RepA free in solution and bound to the operator and to two distinct iteron dsDNA oligonucleotides were determined. These provide indications that in addition to the monomeric RepA-iteron complex a stable dimeric RepA-iteron complex can also exist. .

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