Roberto Galletto, Ph.D.

Associate Professor
Biochemistry and Molecular Biophysics

Biochemistry, Biophysics, and Structural Biology Program

  • 314-362-4368

  • 252 McDonnell Sciences


  • Mechanistic studies of DNA motor proteins; single Molecule Biochemistry

Research Abstract:

The role of DNA helicases in promoting progression of DNA replication through sites that are difficult to replicate is of particular importance for our understanding of maintenance of genomic stability. During each cell cycle, DNA replication needs to overcome multiple obstacles, such as proteins tightly bound to DNA, DNA secondary structures, and damaged DNA. The long-term goal of our research is to understand the activity of accessory helicases at such obstacles in general, but particularly at telomeres, which are known to impede replication and whose integrity is fundamental to genome stability.
One additional goal of our research is to understand how telomeres are organized and regulated. Telomeres can form distinct globules or assemble into larger structures. Understanding the underlying mechanisms that impart telomeres with their globular and dynamic character is key to explaining how telomeres shelter the ends of chromosomes.
In our studies we employ a broad range of techniques, ranging from classical biochemistry approaches to quantitative biophysical techniques both in ensemble and at single-molecule level.

Selected Publications:

Singh, S. P., Kukshal, V., and Galletto, R. (2019) A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt. J Biol Chem

Singh, S. P., Kukshal, V., De Bona, P., Antony, E., and Galletto, R. (2018) The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers. Nucleic Acids Res 46, 7193-7205 PMCID: PMC6101547

Geronimo, C. L., Singh, S. P., Galletto, R., and Zakian, V. A. (2018) The signature motif of the Saccharomyces cerevisiae Pif1 DNA helicase is essential in vivo for mitochondrial and nuclear functions and in vitro for ATPase activity. Nucleic Acids Res 46, 8357-8370 PMCID: PMC6144861

Dahan, D., Tsirkas, I., Dovrat, D., Sparks, M. A., Singh, S. P., Galletto, R., and Aharoni, A. (2018) Pif1 is essential for efficient replisome progression through lagging strand G-quadruplex DNA secondary structures. Nucleic Acids Res 46, 11847-11857 PMC6294490

Sokoloski, J. E., Kozlov, A. G., Galletto, R., and Lohman, T. M. (2016) Chemo-mechanical pushing of proteins along single-stranded DNA. Proc Natl Acad Sci U S A 113, 6194-6199 PMC4896671

Singh, S. P., Koc, K. N., Stodola, J. L., and Galletto, R. (2016) A Monomer of Pif1 Unwinds Double-Stranded DNA and It Is Regulated by the Nature of the Non-Translocating Strand at the 3`-End. J Mol Biol 428, 1053-1067 PMC4826290

Koc, K. N., Singh, S. P., Stodola, J. L., Burgers, P. M., and Galletto, R. (2016) Pif1 removes a Rap1-dependent barrier to the strand displacement activity of DNA polymerase delta. Nucleic Acids Res 44, 3811-3819 PMC4856994

Koc, K. N., Stodola, J. L., Burgers, P. M., and Galletto, R. (2015) Regulation of yeast DNA polymerase delta-mediated strand displacement synthesis by 5`-flaps. Nucleic Acids Res 43, 4179-4190 PMC4417170

Feldmann, E. A., Koc, K. N., and Galletto, R. (2015) Alternative arrangements of telomeric recognition sites regulate the binding mode of the DNA-binding domain of yeast Rap1. Biophys Chem 198, 1-8 PMC4459892

Feldmann, E. A., De Bona, P., and Galletto, R. (2015) The wrapping loop and Rap1 C-terminal (RCT) domain of yeast Rap1 modulate access to different DNA binding modes. J Biol Chem 290, 11455-11466 PMC4416850

Last Updated: 2/22/2019 8:53:46 AM

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