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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Related Experiment Video

Updated: Aug 30, 2025

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases
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Rtt105 regulates RPA function by configurationally stapling the flexible domains.

Sahiti Kuppa1, Jaigeeth Deveryshetty1, Rahul Chadda1

  • 1Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO, 63104, USA.

Nature Communications
|September 2, 2022
PubMed
Summary
This summary is machine-generated.

Rtt105, a molecular chaperone, stabilizes Replication Protein A (RPA) complexes on single-stranded DNA (ssDNA) and prevents their premature interactions. This ensures RPA is available for DNA repair and replication when needed.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Replication Protein A (RPA) is crucial for DNA metabolism, binding single-stranded DNA (ssDNA) and interacting with numerous proteins.
  • RPA's functions in DNA replication, repair, and recombination are tightly regulated.
  • Rtt105 is a known regulator of RPA's nuclear localization.

Purpose of the Study:

  • To elucidate the mechanism by which Rtt105 interacts with and regulates RPA.
  • To understand Rtt105's role in preventing spurious RPA interactions.
  • To investigate how Rtt105 modulates RPA-ssDNA filament formation and stability.

Main Methods:

  • Biochemical assays to study Rtt105-RPA interactions.
  • Analysis of RPA-ssDNA filament formation and stability.
  • Investigation of Rtt105's effect on RPA-interacting protein binding.

Main Results:

  • Rtt105 binds to RPA, acting as a conformational stabilizer.
  • Rtt105 inhibits RPA binding to Rad52 in the absence of ssDNA, preventing off-target protein interactions.
  • Rtt105 promotes RPA-ssDNA filament formation and stabilizes these filaments by inhibiting RPA exchange activity.

Conclusions:

  • Rtt105 sequesters free RPA in the nucleus, preventing premature interactions with other proteins.
  • Rtt105 plays a dual role: preventing inappropriate RPA binding and stabilizing RPA-ssDNA complexes at DNA lesion sites.
  • These findings reveal a novel regulatory mechanism for RPA function in DNA metabolism.