Neither Two-State nor Three-State: Dimerization of Lambda Cro Repressor.
Lambda Cro repressor is one of the best studied dimeric transcription factors. However, there has still been an unsettled debate for decades about whether it is a two-state dimer or three-state dimer. We provide a new mechanism model that can reconcile these seemingly conflicting (mutually exclusive) experimental results. From simulations with all-atom structure-based model, we observe that the dimerization process of Lambda Cro repressor starts from one folded monomer with one unfolded monomer. Intrasubunit folding and intersubunit binding are partially coupled, in a fly casting manner.
John
J
Yao
∥State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, People's Republic of China.
Jin
J
Wang
D010582:Bacteriophage lambda / Q000378:metabolism*; D019281:Dimerization; D056004:Molecular Dynamics Simulation; D017510:Protein Folding; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry / Q000378:metabolism*
D012097:Repressor Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins
all-atom structure-based model; coupled binding-folding; fly casting; free energy landscape; lambda cro repressor; protein dimerization