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Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Biophys+Rev 2016 ; 8 (Suppl 1): 123-33 Nephropedia Template TP
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Protein-induced DNA linking number change by sequence-specific DNA binding proteins and its biological effects #MMPMID28510217
Leng F
Biophys Rev 2016[Nov]; 8 (Suppl 1): 123-33 PMID28510217show ga
Sequence-specific DNA-binding proteins play essential roles in many fundamental biological events such as DNA replication, recombination, and transcription. One common feature of sequence-specific DNA-binding proteins is to introduce structural changes to their DNA recognition sites including DNA-bending and DNA linking number change (?Lk). In this article, I review recent progress in studying protein-induced ?Lk by several sequence-specific DNA-binding proteins, such as E. coli cAMP receptor protein (CRP) and lactose repressor (LacI). It was demonstrated recently that protein-induced ?Lk is an intrinsic property for sequence-specific DNA-binding proteins and does not correlate to protein-induced other structural changes, such as DNA bending. For instance, although CRP bends its DNA recognition site by 90°, it was not able to introduce a ?Lk to it. However, LacI was able to simultaneously bend and introduce a ?Lk to its DNA binding sites. Intriguingly, LacI also constrained superhelicity within LacI?lac O1 complexes if (?) supercoiled DNA templates were provided. I also discuss how protein-induced ?Lk help sequence-specific DNA-binding proteins regulate their biological functions. For example, it was shown recently that LacI utilizes the constrained superhelicity (?Lk) in LacI-lac O1 complexes and serves as a topological barrier to constrain free, unconstrained (?) supercoils within the 401-bp DNA loop. These constrained (?) supercoils enhance LacI?s binding affinity and therefore the repression of the lac promoter. Other biological functions include how DNA replication initiators ? O and DnaA use the induced ?Lk to open/melt bacterial DNA replication origins.