A quantitative study of lambda-phage SWITCH and its components.
We propose what we believe is a new model to quantitatively describe the lambda-phage SWITCH system. The model incorporates facilitated transfer mechanism of transcription factor, which can be simplified into a two-step reaction. We first sequentially obtain two indispensable parameters by fitting our model to experimental data of two simple systems, and then apply them to study the natural lambda-SWITCH system. By incorporating the facilitated transfer mechanism, we find that in RecA(-) host Escherichia coli, the wild-type lambda-lysogenic state is in a monostable regime rather than in a bistable regime. Furthermore, the model explains the weak role of Cro protein and probably sheds light on the evolution of lambda-Cro protein, which is known to be structurally distinct from the other Cros in lambdoid family members.
Lou
Chunbo
C
Center for Theoretical Biology and School of Physics, Peking University, Beijing, 100871, China.
Yang
Xiaojing
X
Liu
Xili
X
He
Bin
B
Ouyang
Qi
Q
D010582:Bacteriophage lambda / Q000737:chemistry* / Q000235:genetics*; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics; D019143:Evolution, Molecular; D005812:Genes, Switch / Q000235:genetics*; D008956:Models, Chemical; D008957:Models, Genetic; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics*; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins