D
IPR045085

DNA polymerase III, subunit gamma/tau, helical lid domain

InterPro entry
Short nameHLD_clamp_pol_III_gamma_tau
Overlapping
homologous
superfamilies
 

Description

DNA polymerase III subunit gamma/tau is part of the DNA polymerase III holoenzyme. Gamma and tau subunits are isoforms, both containing the helical lid domain. Gamma interacts with the delta subunit to transfer the beta subunit on the DNA while tau serves as a scaffold to help in the dimerization of the core complex. Both are members of the clamp-loader clade of the AAA superfamily
[1, 2]
.

References

1.Review: The lord of the rings: Structure and mechanism of the sliding clamp loader. Kelch BA. Biopolymers 105, 532-46, (2016). PMID: 26918303

2.The ATP sites of AAA+ clamp loaders work together as a switch to assemble clamps on DNA. Marzahn MR, Hayner JN, Finkelstein J, O'Donnell M, Bloom LB. J Biol Chem 289, 5537-48, (2014). PMID: 24436332

Further reading

3. Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit. Podobnik M, Weitze TF, O'Donnell M, Kuriyan J. Structure 11, 253-63, (2003). View articlePMID: 12623013

4. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Jeruzalmi D, O'Donnell M, Kuriyan J. Cell 106, 429-41, (2001). View articlePMID: 11525729

5. Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex. Kazmirski SL, Podobnik M, Weitze TF, O'Donnell M, Kuriyan J. Proc. Natl. Acad. Sci. U.S.A. 101, 16750-5, (2004). View articlePMID: 15556993

6. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J. Cell 137, 659-71, (2009). View articlePMID: 19450514

Cross References

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