A model for transition of 5'-nuclease domain of DNA polymerase I from inert to active modes

Bacteria contain DNA polymerase I (PolI), a single polypeptide chain consisting of ∼930 residues, possessing DNA-dependent DNA polymerase, 3'-5' proofreading and 5'-3' exonuclease (also known as flap endonuclease) activities. PolI is particularly important in the processing of Ok...

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Veröffentlicht in:	PloS one 2011-01, Vol.6 (1), p.e16213-e16213
Hauptverfasser:	Xie, Ping, Sayers, Jon R
Format:	Artikel
Sprache:	eng
Schlagworte:	Analysis Bacteria Bacterial Proteins - chemistry Biology Catalytic Domain Cleavage Collaboration Deoxyribonucleic acid DNA DNA - metabolism DNA polymerase DNA Polymerase I - chemistry DNA synthesis DNA-directed DNA polymerase E coli Endonuclease Enzymes Exonuclease Experimental data Laboratories Ligases Models, Chemical Models, Theoretical Nuclease Nucleases Okazaki fragments Phosphodiesterase I - chemistry Physics Polymerase chain reaction Proofreading Proteins Spectrum analysis Streptococcus infections Thermus aquaticus
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