Article Abstract:
DNA polymerase III is a complex protein that is composed of ten subunits and is responsible for replicating the DNA strand as it unwinds into two parallel strands. The replication of two strands has been visualized as a simultaneous event that is initiated when a beta subunit forms a ring around the DNA and uncoils it. One strand is replicated directly while the other undergoes a sequential replication of fragments before being joined to form one strand. The efficiency of these mechanisms may be due to the close interactions between subunits and the DNA strands being replicated.
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Article Abstract:
The large size of oligomers produced during HK97 maturation is the reason why this bacteriophage's polypeptides are excluded from polyacrylamide gels after denaturation. Their enlargement is attributed to the intertwining of pentamer and hexamer rings before the covalent cross-linking of the bacteriophage's polypeptides. The adjacent protein rings catenate into a network similar to a chainmail armor. Such a structure is supported by experimental findings on the properties of these bacteriophages.
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Article Abstract:
A study was conducted on the crystal structure of a pol alpha family replication DNA polymerase form bacteriophage RB69. Results show that although 2.8 A resolution crystal structure of the bacteriophage have similar features with other polymerases, they also exhibit several differences. This include is the location of one the three carboxylates needed for nucleotidyl transfer.
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