Inching over hurdles: how DNA helicases move on crowded lattices.
Many of the genome maintenance transactions require continuous progression of molecular motors along single or double stranded DNA (dsDNA) molecule. DNA, however, is rarely found in the cell in its bare form. Structural proteins organize dsDNA and control its accessibility to molecular machines of DNA replication, repair, recombination and transcription. Single-stranded DNA (ssDNA) is sequestered by ssDNA binding proteins, which protect it from degradation, modification and undesired transactions. Appreciation of how molecular machines compete with these stationary blocks and with each other for the access to DNA is important for our understanding of the mechanisms underlying genome maintenance. This understanding in turn establishes the molecular basis of various human diseases resulting from defects in molecular motors and their ability to navigate in crowded intracellular environments. By building upon our recent finding that it is possible for a helicase translocating on ssDNA to bypass a stationary bound protein without displacing it, we discuss potential outcomes of collisions between DNA helicases and ssDNA binding proteins. We then propose that the selective ability of some helicases to bypass or displace a specific ssDNA binding protein may be important for activation of these enzymes for particular DNA maintenance tasks.
Spies
Maria
M
Howard Hughes Medical Institute, Department of Biochemistry and Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA. mspies@life.illinois.edu
Ha
Taekjip
T
D004265:DNA Helicases / Q000378:metabolism*; D004261:DNA Replication; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins / Q000378:metabolism; D006801:Humans
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D004265:DNA Helicases