Home Biochemistry Comparing the Affinity of GTPase-binding Proteins using Competition Assays
Biochemistry JoVE (Open Access) Citable · DOI

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

DOI: 10.3791/53254-v
What you'll learn
  • Purify and prepare GTPase-binding proteins for affinity studies
  • Load and control nucleotide state of Rho-family GTPases
  • Execute competition binding assays to measure relative affinities
  • Quantify and compare binding affinities between competing proteins
Protocol

This protocol compares the relative affinities of binding partners for Rho-family GTPases, including Rac1. In vivo, Rac1-binding proteins compete for a single binding interface, the conformation of which is dictated by a bound nucleotide. The nucleotide is both important and difficult to control experimentally, due to the high hydrolysis rate.

Difficulty
advanced
Total time
~4–6 hours per experiment (protein purification + nucleotide loading + competition assay)
Biosafety
BSL-1

Steps

1
Purify GTPase-binding proteins from expression system

Express and isolate recombinant Rho-family GTPase-binding proteins (e.g., RCC2, Coronin-1C) using standard protein purification techniques. Ensure high purity for subsequent binding assays.

▶ 01:38
2
Load GTPase with controlled nucleotide state

Exchange nucleotides on purified Rac1 or related GTPase to achieve a defined, stable nucleotide-bound conformation. Control for nucleotide hydrolysis to maintain consistent experimental conditions.

▶ 04:45
3
Perform competition binding assay

Incubate nucleotide-loaded GTPase with multiple binding partners simultaneously to measure competition for the shared binding interface. Quantify relative binding by detecting which protein occupies the GTPase binding site.

▶ 06:32
4
Determine relative binding affinities from competition data

Analyze competition assay results to calculate and compare the relative affinities of RCC2, Coronin-1C, and other binding partners for Rac1. Express results quantitatively to rank binding strength.

▶ 08:42
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