Structure and Functions of DNA Polymerase III Holoenzyme of E. coli
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DNA polymerase III holoenzyme is the principal replicative                      enzyme of E. coli.  High catalytic rates are achieved by                        having the polymerase subunit (called alpha) of the 10-                         subunit enzyme clamped to the template by auxiliary subunits;                   its high fidelity of replication is achieved by complexing of                   the alpha subunit with the epsilon subunit to enable                            effective proofreading at the growing end of the chain.  The                    holoenzyme is in fact part of a more complex machine which                      contains two polymerase subunits and together with priming                      proteins and helicases may constitute a "replisome."  Seated                    at the replication fork of a chromosome, the replisome may                      effect a relatively concurrent replication of both strands of                   the duplex chromosome rather than the spasmodic, jerky,                         semidiscontinuous model now in use.  Toward establishing the                    detailed structure and individual functions of several forms                    of this extraordinary polymerase molecule, various techniques                   of genetic engineering, protein isolation, immunocyto-                          chemistry, electron microscopy and enzymology will be used.                     The significance of understanding replication in molecular                      detail lies in its application toward the development of                        drugs to interrupt the process in proliferative diseases,                       such as cancer, and the acquisition of new insights into                        growth processes and their aberrations.
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{'Code': '1166', 'Text': 'MOLECULAR BIOCHEMISTRY'}
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