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In Vivo Architecture and Action of Bacterial Structural Maintenance of Chromosome Proteins

Making a Move Structural Maintenance of Chromosome (SMC) complexes act ubiquitously in chromosome processing in all domains of life, but their mode of action in living cells has remained an enigma. Badrinarayanan et al. (p. 528) used noninvasive millisecond single-molecule imaging to understand SMC complex molecular biochemistry in living bacterial cells with super-resolution spatial precision. Escherichia coli SMC complexes, which are important for chromosome segregation, formed dimers that bound to DNA in an adenosine triphosphate (ATP)–dependent manner and that could be released upon ATP-hydrolysis. By functioning in pairs, the complexes are likely to be able to undergo multiple cycles of ATP-hydrolysis without being released from DNA. SMC proteins form a dimer of adenosine triphosphate (ATP)–bound dimers, which translate ATP hydrolysis into mechanical DNA remodeling. SMC (structural maintenance of chromosome) proteins act ubiquitously in chromosome processing. In Escherichia coli, the SMC complex MukBEF plays roles in chromosome segregation and organization. We used single-molecule millisecond multicolor fluorescence microscopy of live bacteria to reveal that a dimer of dimeric fluorescent MukBEF molecules acts as the minimal functional unit. On average, 8 to 10 of these complexes accumulated as “spots” in one to three discrete chromosome-associated regions of the cell, where they formed higher-order structures. Functional MukBEF within spots exchanged with freely diffusing complexes at a rate of one complex about every 50 seconds in reactions requiring adenosine triphosphate (ATP) hydrolysis. Thus, by functioning in pairs, MukBEF complexes may undergo multiple cycles of ATP hydrolysis without being released from DNA, analogous to the behavior of well-characterized molecular motors.