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A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.
Georgescu, R. E. et al. Structure of a sliding clamp on DNA.
It can capture the newly released A subunit, thus moving the sliding clamp up by ~2.5 base pairs.
Laurence, T. A. et al. Motion of a DNA sliding clamp observed by single molecule fluorescence spectroscopy.
Kelch, B. A., Makino, D. L., O'Donnell, M. & Kuriyan, J. How a DNA polymerase clamp loader opens a sliding clamp.
(C) Six identical AAA+ modules attached to a sliding clamp on DNA will form a filament in the presence of ATP.
Snowden, T., Acharya, S., Butz, C., Berardini, M. & Fishel, R. hMSH4-hMSH5 recognizes Holliday junctions and forms a meiosis-specific sliding clamp that embraces homologous chromosomes.
Processive chromosomal replication requires ring-shaped sliding clamp factors that encircle DNA and anchor polymerases and other proteins of the replisome.
To extend our understanding of the structure/function relationship of the sliding clamp, we solved the crystal structure of the sliding clamp from Mycobacterium tuberculosis (M. tuberculosis), a human pathogen that causes most cases of tuberculosis (TB).
Thus, the sliding clamp seems to have evolved as an efficient mechanism for ensuring proficient DNA replication.
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For processivity, PolIIIα binds to the DNA sliding clamp (β subunit) (Stukenberg et al., 1991).
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