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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2019.1
- 수록면
- 613 - 619 (7page)
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Background Among several key protein–protein and protein–DNA interactions within the replisome, the interaction between β-clamp and the DNA polymerase (Pol) III is of crucial importance. This interaction is mediated by a five or six-residue conserved sequence of the DnaE subunit of Pol III, referred to as the Clamp Binding Motif (CBM). In E. coli, DnaE contains two CBMs designated as e-CBM and i-CBM. A consensus sequence (QL[S/D]LF) for the CBMs has previously been proposed and studies involving mutagenesis of both the CBMs have evaluated their protein-binding properties. Surface Plasmon Resonance has been used to show that replacing i-CBM in DnaE with the consensus sequence enhances its binding to β-clamp 120-fold. Objective The current study was aimed to evaluate in vivo interaction between DnaE bearing the consensus i-CBM and β-clamp. Method The C-terminal 405 residues of DnaE, bearing either the consensus i-CBM or the WT i-CBM, with β-clamp were co-expressed in E. coli followed by co-purification of the protein complexes. The interaction was assessed by the ability of the co-expressed proteins to form stable complexes during both affinity and gel filtration chromatography. Result The interaction of β-clamp with DnaEΔ755M containing the consensus i-CBM was found to be more stable than with WT DnaEΔ755, consistent with the in vitro data previously reported. Conclusion The presence of the pieces of sheared DNA generated during sonication promote the interaction of DnaEΔ755M with β-clamp by binding the OB-fold of DnaEΔ755M and β-clamp and serves as a bridge between them.
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참고문헌 (20)
참고문헌 신청
Burnouf DY / 2004 / Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competition between replicative and translesion DNA polymerases / J Mol Biol 335:1187~1197
Dalrymple BP / 2001 / A universal protein–protein interaction motif in the eubacterial DNA replication and repair systems / Proc Natl Acad Sci 98:11627~11632
Prescott L. Deininger / 1983 / Random subcloning of sonicated DNA: Application to shotgun DNA sequence analysis / Analytical Biochemistry 129(1):216~223
Doherty AJ / 1996 / The helix-hairpin-helix DNA-binding motif : a structural basis for non-sequence-specific recognition of DNA / Nucleic Acids Res 24:2488~2497
Dohrmann PR / 2005 / A bipartite polymerase-processivity factor interaction : only the internal β binding site of the α subunit is required for processive replication by the DNA polymerase III holoenzyme / J Mol Biol 350:228~239
Dalrymple BP / 2001 / A universal protein–protein interaction motif in the eubacterial DNA replication and repair systems / Proc Natl Acad Sci 98:11627~11632
Prescott L. Deininger / 1983 / Random subcloning of sonicated DNA: Application to shotgun DNA sequence analysis / Analytical Biochemistry 129(1):216~223
Doherty AJ / 1996 / The helix-hairpin-helix DNA-binding motif : a structural basis for non-sequence-specific recognition of DNA / Nucleic Acids Res 24:2488~2497
Dohrmann PR / 2005 / A bipartite polymerase-processivity factor interaction : only the internal β binding site of the α subunit is required for processive replication by the DNA polymerase III holoenzyme / J Mol Biol 350:228~239
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